---
_id: '11100'
abstract:
- lang: eng
text: Eukaryotic cell function depends on the physical separation of nucleoplasmic
and cytoplasmic components by the nuclear envelope (NE). Molecular communication
between the two compartments involves active, signal-mediated trafficking, a function
that is exclusively performed by nuclear pore complexes (NPCs). The individual
NPC components and the mechanisms that are involved in nuclear trafficking are
well documented and have become textbook knowledge. However, in addition to their
roles as nuclear gatekeepers, NPC components-nucleoporins-have been shown to have
critical roles in chromatin organization and gene regulation. These findings have
sparked new enthusiasm to study the roles of this multiprotein complex in nuclear
organization and explore novel functions that in some cases appear to go beyond
a role in transport. Here, we discuss our present view of NPC biogenesis, which
is tightly linked to proper cell cycle progression and cell differentiation. In
addition, we summarize new data suggesting that NPCs represent dynamic hubs for
the integration of gene regulation and nuclear transport processes.
article_processing_charge: No
article_type: original
author:
- first_name: M.
full_name: Capelson, M.
last_name: Capelson
- first_name: C.
full_name: Doucet, C.
last_name: Doucet
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: 'Capelson M, Doucet C, Hetzer M. Nuclear pore complexes: Guardians of the nuclear
genome. Cold Spring Harbor Symposia on Quantitative Biology. 2011;75:585-597.
doi:10.1101/sqb.2010.75.059'
apa: 'Capelson, M., Doucet, C., & Hetzer, M. (2011). Nuclear pore complexes:
Guardians of the nuclear genome. Cold Spring Harbor Symposia on Quantitative
Biology. Cold Spring Harbor Laboratory Press. https://doi.org/10.1101/sqb.2010.75.059'
chicago: 'Capelson, M., C. Doucet, and Martin Hetzer. “Nuclear Pore Complexes: Guardians
of the Nuclear Genome.” Cold Spring Harbor Symposia on Quantitative Biology.
Cold Spring Harbor Laboratory Press, 2011. https://doi.org/10.1101/sqb.2010.75.059.'
ieee: 'M. Capelson, C. Doucet, and M. Hetzer, “Nuclear pore complexes: Guardians
of the nuclear genome,” Cold Spring Harbor Symposia on Quantitative Biology,
vol. 75. Cold Spring Harbor Laboratory Press, pp. 585–597, 2011.'
ista: 'Capelson M, Doucet C, Hetzer M. 2011. Nuclear pore complexes: Guardians of
the nuclear genome. Cold Spring Harbor Symposia on Quantitative Biology. 75, 585–597.'
mla: 'Capelson, M., et al. “Nuclear Pore Complexes: Guardians of the Nuclear Genome.”
Cold Spring Harbor Symposia on Quantitative Biology, vol. 75, Cold Spring
Harbor Laboratory Press, 2011, pp. 585–97, doi:10.1101/sqb.2010.75.059.'
short: M. Capelson, C. Doucet, M. Hetzer, Cold Spring Harbor Symposia on Quantitative
Biology 75 (2011) 585–597.
date_created: 2022-04-07T07:53:18Z
date_published: 2011-04-18T00:00:00Z
date_updated: 2022-07-18T08:54:23Z
day: '18'
doi: 10.1101/sqb.2010.75.059
extern: '1'
external_id:
pmid:
- '21502404'
intvolume: ' 75'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
month: '04'
oa_version: None
page: 585-597
pmid: 1
publication: Cold Spring Harbor Symposia on Quantitative Biology
publication_identifier:
isbn:
- '9781936113071'
issn:
- 0091-7451
- 1943-4456
publication_status: published
publisher: Cold Spring Harbor Laboratory Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Nuclear pore complexes: Guardians of the nuclear genome'
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 75
year: '2011'
...
---
_id: '12199'
abstract:
- lang: eng
text: The four microsporangia of the flowering plant anther develop from archesporial
cells in the L2 of the primordium. Within each microsporangium, developing microsporocytes
are surrounded by concentric monolayers of tapetal, middle layer and endothecial
cells. How this intricate array of tissues, each containing relatively few cells,
is established in an organ possessing no formal meristems is poorly understood.
We describe here the pivotal role of the LRR receptor kinase EXCESS MICROSPOROCYTES
1 (EMS1) in forming the monolayer of tapetal nurse cells in Arabidopsis. Unusually
for plants, tapetal cells are specified very early in development, and are subsequently
stimulated to proliferate by a receptor-like kinase (RLK) complex that includes
EMS1. Mutations in members of this EMS1 signalling complex and its putative ligand
result in male-sterile plants in which tapetal initials fail to proliferate. Surprisingly,
these cells continue to develop, isolated at the locular periphery. Mutant and
wild-type microsporangia expand at similar rates and the ‘tapetal’ space at the
periphery of mutant locules becomes occupied by microsporocytes. However, induction
of late expression of EMS1 in the few tapetal initials in ems1 plants results
in their proliferation to generate a functional tapetum, and this proliferation
suppresses microsporocyte number. Our experiments also show that integrity of
the tapetal monolayer is crucial for the maintenance of the polarity of divisions
within it. This unexpected autonomy of the tapetal ‘lineage’ is discussed in the
context of tissue development in complex plant organs, where constancy in size,
shape and cell number is crucial.
acknowledgement: 'We thank the following for providing mutant lines and reagents:
Hong Ma, De Ye, Sacco De Vries, and Rod Scott for providing the pA9::Barnase lines
and information on A9 expression patterns. Carla Galinha and Paolo Piazza gave valuable
help with in situ hybridisation and qRT-PCR, respectively, and we acknowledge Qing
Zhang, Helen Prescott and Matthew Dicks for providing excellent technical assistance.
We are indebted to Miltos Tsiantis and Angela Hay for helpful discussion, and the
research was funded by Oxford University through a Clarendon Scholarship to X.F.,
with additional financial support from Magdalen College (Oxford).'
article_processing_charge: No
article_type: original
author:
- first_name: Xiaoqi
full_name: Feng, Xiaoqi
id: e0164712-22ee-11ed-b12a-d80fcdf35958
last_name: Feng
orcid: 0000-0002-4008-1234
- first_name: Hugh G.
full_name: Dickinson, Hugh G.
last_name: Dickinson
citation:
ama: Feng X, Dickinson HG. Tapetal cell fate, lineage and proliferation in the Arabidopsis
anther. Development. 2010;137(14):2409-2416. doi:10.1242/dev.049320
apa: Feng, X., & Dickinson, H. G. (2010). Tapetal cell fate, lineage and proliferation
in the Arabidopsis anther. Development. The Company of Biologists. https://doi.org/10.1242/dev.049320
chicago: Feng, Xiaoqi, and Hugh G. Dickinson. “Tapetal Cell Fate, Lineage and Proliferation
in the Arabidopsis Anther.” Development. The Company of Biologists, 2010.
https://doi.org/10.1242/dev.049320.
ieee: X. Feng and H. G. Dickinson, “Tapetal cell fate, lineage and proliferation
in the Arabidopsis anther,” Development, vol. 137, no. 14. The Company
of Biologists, pp. 2409–2416, 2010.
ista: Feng X, Dickinson HG. 2010. Tapetal cell fate, lineage and proliferation in
the Arabidopsis anther. Development. 137(14), 2409–2416.
mla: Feng, Xiaoqi, and Hugh G. Dickinson. “Tapetal Cell Fate, Lineage and Proliferation
in the Arabidopsis Anther.” Development, vol. 137, no. 14, The Company
of Biologists, 2010, pp. 2409–16, doi:10.1242/dev.049320.
short: X. Feng, H.G. Dickinson, Development 137 (2010) 2409–2416.
date_created: 2023-01-16T09:21:54Z
date_published: 2010-07-15T00:00:00Z
date_updated: 2023-05-08T10:57:11Z
day: '15'
department:
- _id: XiFe
doi: 10.1242/dev.049320
extern: '1'
external_id:
pmid:
- '20570940'
intvolume: ' 137'
issue: '14'
keyword:
- Developmental Biology
- Molecular Biology
- Anther Tapetum
- Arabidopsis
- Cell Fate Establishment
- EMS1
- Reproductive Cell Lineage
language:
- iso: eng
month: '07'
oa_version: None
page: 2409-2416
pmid: 1
publication: Development
publication_identifier:
issn:
- 1477-9129
- 0950-1991
publication_status: published
publisher: The Company of Biologists
quality_controlled: '1'
scopus_import: '1'
status: public
title: Tapetal cell fate, lineage and proliferation in the Arabidopsis anther
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 137
year: '2010'
...
---
_id: '8473'
abstract:
- lang: eng
text: β2-microglobulin (β2m), the light chain of class I major histocompatibility
complex, is responsible for the dialysis-related amyloidosis and, in patients
undergoing long term dialysis, the full-length and chemically unmodified β2m converts
into amyloid fibrils. The protein, belonging to the immunoglobulin superfamily,
in common to other members of this family, experiences during its folding a long-lived
intermediate associated to the trans-to-cis isomerization of Pro-32 that has been
addressed as the precursor of the amyloid fibril formation. In this respect, previous
studies on the W60G β2m mutant, showing that the lack of Trp-60 prevents fibril
formation in mild aggregating condition, prompted us to reinvestigate the refolding
kinetics of wild type and W60G β2m at atomic resolution by real-time NMR. The
analysis, conducted at ambient temperature by the band selective flip angle short
transient real-time two-dimensional NMR techniques and probing the β2m states
every 15 s, revealed a more complex folding energy landscape than previously reported
for wild type β2m, involving more than a single intermediate species, and shedding
new light into the fibrillogenic pathway. Moreover, a significant difference in
the kinetic scheme previously characterized by optical spectroscopic methods was
discovered for the W60G β2m mutant.
article_processing_charge: No
article_type: original
author:
- first_name: Alessandra
full_name: Corazza, Alessandra
last_name: Corazza
- first_name: Enrico
full_name: Rennella, Enrico
last_name: Rennella
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Maria Chiara
full_name: Mimmi, Maria Chiara
last_name: Mimmi
- first_name: Thomas
full_name: Cutuil, Thomas
last_name: Cutuil
- first_name: Sara
full_name: Raimondi, Sara
last_name: Raimondi
- first_name: Sofia
full_name: Giorgetti, Sofia
last_name: Giorgetti
- first_name: Federico
full_name: Fogolari, Federico
last_name: Fogolari
- first_name: Paolo
full_name: Viglino, Paolo
last_name: Viglino
- first_name: Lucio
full_name: Frydman, Lucio
last_name: Frydman
- first_name: Maayan
full_name: Gal, Maayan
last_name: Gal
- first_name: Vittorio
full_name: Bellotti, Vittorio
last_name: Bellotti
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Gennaro
full_name: Esposito, Gennaro
last_name: Esposito
citation:
ama: Corazza A, Rennella E, Schanda P, et al. Native-unlike long-lived intermediates
along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed
by real-time two-dimensional NMR. Journal of Biological Chemistry. 2010;285(8):5827-5835.
doi:10.1074/jbc.m109.061168
apa: Corazza, A., Rennella, E., Schanda, P., Mimmi, M. C., Cutuil, T., Raimondi,
S., … Esposito, G. (2010). Native-unlike long-lived intermediates along the folding
pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional
NMR. Journal of Biological Chemistry. American Society for Biochemistry
& Molecular Biology. https://doi.org/10.1074/jbc.m109.061168
chicago: Corazza, Alessandra, Enrico Rennella, Paul Schanda, Maria Chiara Mimmi,
Thomas Cutuil, Sara Raimondi, Sofia Giorgetti, et al. “Native-Unlike Long-Lived
Intermediates along the Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin
Revealed by Real-Time Two-Dimensional NMR.” Journal of Biological Chemistry.
American Society for Biochemistry & Molecular Biology, 2010. https://doi.org/10.1074/jbc.m109.061168.
ieee: A. Corazza et al., “Native-unlike long-lived intermediates along the
folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time
two-dimensional NMR,” Journal of Biological Chemistry, vol. 285, no. 8.
American Society for Biochemistry & Molecular Biology, pp. 5827–5835, 2010.
ista: Corazza A, Rennella E, Schanda P, Mimmi MC, Cutuil T, Raimondi S, Giorgetti
S, Fogolari F, Viglino P, Frydman L, Gal M, Bellotti V, Brutscher B, Esposito
G. 2010. Native-unlike long-lived intermediates along the folding pathway of the
amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR.
Journal of Biological Chemistry. 285(8), 5827–5835.
mla: Corazza, Alessandra, et al. “Native-Unlike Long-Lived Intermediates along the
Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin Revealed by Real-Time
Two-Dimensional NMR.” Journal of Biological Chemistry, vol. 285, no. 8,
American Society for Biochemistry & Molecular Biology, 2010, pp. 5827–35,
doi:10.1074/jbc.m109.061168.
short: A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi,
S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher,
G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835.
date_created: 2020-09-18T10:11:23Z
date_published: 2010-02-19T00:00:00Z
date_updated: 2021-01-12T08:19:31Z
day: '19'
doi: 10.1074/jbc.m109.061168
extern: '1'
intvolume: ' 285'
issue: '8'
keyword:
- Cell Biology
- Biochemistry
- Molecular Biology
language:
- iso: eng
month: '02'
oa_version: None
page: 5827-5835
publication: Journal of Biological Chemistry
publication_identifier:
issn:
- 0021-9258
- 1083-351X
publication_status: published
publisher: American Society for Biochemistry & Molecular Biology
quality_controlled: '1'
status: public
title: Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic
protein β2-Microglobulin revealed by real-time two-dimensional NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 285
year: '2010'
...
---
_id: '11097'
abstract:
- lang: eng
text: The nuclear envelope (NE) is a highly regulated membrane barrier that separates
the nucleus from the cytoplasm in eukaryotic cells. It contains a large number
of different proteins that have been implicated in chromatin organization and
gene regulation. Although the nuclear membrane enables complex levels of gene
expression, it also poses a challenge when it comes to cell division. To allow
access of the mitotic spindle to chromatin, the nucleus of metazoans must completely
disassemble during mitosis, generating the need to re-establish the nuclear compartment
at the end of each cell division. Here, I summarize our current understanding
of the dynamic remodeling of the NE during the cell cycle.
article_processing_charge: No
article_type: original
author:
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Hetzer M. The nuclear envelope. Cold Spring Harbor Perspectives in Biology.
2010;2(3):a000539-a000539. doi:10.1101/cshperspect.a000539
apa: Hetzer, M. (2010). The nuclear envelope. Cold Spring Harbor Perspectives
in Biology. Cold Spring Harbor Laboratory. https://doi.org/10.1101/cshperspect.a000539
chicago: Hetzer, Martin. “The Nuclear Envelope.” Cold Spring Harbor Perspectives
in Biology. Cold Spring Harbor Laboratory, 2010. https://doi.org/10.1101/cshperspect.a000539.
ieee: M. Hetzer, “The nuclear envelope,” Cold Spring Harbor Perspectives in Biology,
vol. 2, no. 3. Cold Spring Harbor Laboratory, pp. a000539–a000539, 2010.
ista: Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology.
2(3), a000539–a000539.
mla: Hetzer, Martin. “The Nuclear Envelope.” Cold Spring Harbor Perspectives
in Biology, vol. 2, no. 3, Cold Spring Harbor Laboratory, 2010, pp. a000539–a000539,
doi:10.1101/cshperspect.a000539.
short: M. Hetzer, Cold Spring Harbor Perspectives in Biology 2 (2010) a000539–a000539.
date_created: 2022-04-07T07:52:49Z
date_published: 2010-02-03T00:00:00Z
date_updated: 2022-07-18T08:53:50Z
day: '03'
doi: 10.1101/cshperspect.a000539
extern: '1'
external_id:
pmid:
- '20300205'
intvolume: ' 2'
issue: '3'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '02'
oa_version: None
page: a000539-a000539
pmid: 1
publication: Cold Spring Harbor Perspectives in Biology
publication_identifier:
issn:
- 1943-0264
publication_status: published
publisher: Cold Spring Harbor Laboratory
quality_controlled: '1'
scopus_import: '1'
status: public
title: The nuclear envelope
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 2
year: '2010'
...
---
_id: '11098'
article_processing_charge: No
article_type: original
author:
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Hetzer M. The role of the nuclear pore complex in aging of post-mitotic cells.
Aging. 2010;2(2):74-75. doi:10.18632/aging.100125
apa: Hetzer, M. (2010). The role of the nuclear pore complex in aging of post-mitotic
cells. Aging. Impact Journals. https://doi.org/10.18632/aging.100125
chicago: Hetzer, Martin. “The Role of the Nuclear Pore Complex in Aging of Post-Mitotic
Cells.” Aging. Impact Journals, 2010. https://doi.org/10.18632/aging.100125.
ieee: M. Hetzer, “The role of the nuclear pore complex in aging of post-mitotic
cells,” Aging, vol. 2, no. 2. Impact Journals, pp. 74–75, 2010.
ista: Hetzer M. 2010. The role of the nuclear pore complex in aging of post-mitotic
cells. Aging. 2(2), 74–75.
mla: Hetzer, Martin. “The Role of the Nuclear Pore Complex in Aging of Post-Mitotic
Cells.” Aging, vol. 2, no. 2, Impact Journals, 2010, pp. 74–75, doi:10.18632/aging.100125.
short: M. Hetzer, Aging 2 (2010) 74–75.
date_created: 2022-04-07T07:52:58Z
date_published: 2010-02-01T00:00:00Z
date_updated: 2022-07-18T08:54:15Z
day: '01'
doi: 10.18632/aging.100125
extern: '1'
external_id:
pmid:
- '20354266'
intvolume: ' 2'
issue: '2'
keyword:
- Cell Biology
- Aging
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.18632/aging.100125
month: '02'
oa: 1
oa_version: Published Version
page: 74-75
pmid: 1
publication: Aging
publication_identifier:
issn:
- 1945-4589
publication_status: published
publisher: Impact Journals
quality_controlled: '1'
scopus_import: '1'
status: public
title: The role of the nuclear pore complex in aging of post-mitotic cells
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 2
year: '2010'
...
---
_id: '11101'
abstract:
- lang: eng
text: In metazoa, nuclear pore complexes (NPCs) assemble from disassembled precursors
into a reforming nuclear envelope (NE) at the end of mitosis and into growing
intact NEs during interphase. Here, we show via RNAi-mediated knockdown that ELYS,
a nucleoporin critical for the recruitment of the essential Nup107/160 complex
to chromatin, is required for NPC assembly at the end of mitosis but not during
interphase. Conversely, the transmembrane nucleoporin POM121 is critical for the
incorporation of the Nup107/160 complex into new assembly sites specifically during
interphase. Strikingly, recruitment of the Nup107/160 complex to an intact NE
involves a membrane curvature-sensing domain of its constituent Nup133, which
is not required for postmitotic NPC formation. Our results suggest that in organisms
with open mitosis, NPCs assemble via two distinct mechanisms to accommodate cell
cycle-dependent differences in NE topology.
article_processing_charge: No
article_type: original
author:
- first_name: Christine M.
full_name: Doucet, Christine M.
last_name: Doucet
- first_name: Jessica A.
full_name: Talamas, Jessica A.
last_name: Talamas
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Doucet CM, Talamas JA, Hetzer M. Cell cycle-dependent differences in nuclear
pore complex assembly in metazoa. Cell. 2010;141(6):1030-1041. doi:10.1016/j.cell.2010.04.036
apa: Doucet, C. M., Talamas, J. A., & Hetzer, M. (2010). Cell cycle-dependent
differences in nuclear pore complex assembly in metazoa. Cell. Elsevier.
https://doi.org/10.1016/j.cell.2010.04.036
chicago: Doucet, Christine M., Jessica A. Talamas, and Martin Hetzer. “Cell Cycle-Dependent
Differences in Nuclear Pore Complex Assembly in Metazoa.” Cell. Elsevier,
2010. https://doi.org/10.1016/j.cell.2010.04.036.
ieee: C. M. Doucet, J. A. Talamas, and M. Hetzer, “Cell cycle-dependent differences
in nuclear pore complex assembly in metazoa,” Cell, vol. 141, no. 6. Elsevier,
pp. 1030–1041, 2010.
ista: Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in
nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.
mla: Doucet, Christine M., et al. “Cell Cycle-Dependent Differences in Nuclear Pore
Complex Assembly in Metazoa.” Cell, vol. 141, no. 6, Elsevier, 2010, pp.
1030–41, doi:10.1016/j.cell.2010.04.036.
short: C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041.
date_created: 2022-04-07T07:53:29Z
date_published: 2010-06-11T00:00:00Z
date_updated: 2022-07-18T08:54:52Z
day: '11'
doi: 10.1016/j.cell.2010.04.036
extern: '1'
external_id:
pmid:
- '20550937'
intvolume: ' 141'
issue: '6'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2010.04.036
month: '06'
oa: 1
oa_version: Published Version
page: 1030-1041
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cell cycle-dependent differences in nuclear pore complex assembly in metazoa
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 141
year: '2010'
...
---
_id: '11102'
abstract:
- lang: eng
text: Nuclear pore complexes have recently been shown to play roles in gene activation;
however their potential involvement in metazoan transcription remains unclear.
Here we show that the nucleoporins Sec13, Nup98, and Nup88, as well as a group
of FG-repeat nucleoporins, bind to the Drosophila genome at functionally distinct
loci that often do not represent nuclear envelope contact sites. Whereas Nup88
localizes to silent loci, Sec13, Nup98, and a subset of FG-repeat nucleoporins
bind to developmentally regulated genes undergoing transcription induction. Strikingly,
RNAi-mediated knockdown of intranuclear Sec13 and Nup98 specifically inhibits
transcription of their target genes and prevents efficient reactivation of transcription
after heat shock, suggesting an essential role of NPC components in regulating
complex gene expression programs of multicellular organisms.
article_processing_charge: No
article_type: original
author:
- first_name: Maya
full_name: Capelson, Maya
last_name: Capelson
- first_name: Yun
full_name: Liang, Yun
last_name: Liang
- first_name: Roberta
full_name: Schulte, Roberta
last_name: Schulte
- first_name: William
full_name: Mair, William
last_name: Mair
- first_name: Ulrich
full_name: Wagner, Ulrich
last_name: Wagner
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. Chromatin-bound
nuclear pore components regulate gene expression in higher eukaryotes. Cell.
2010;140(3):372-383. doi:10.1016/j.cell.2009.12.054
apa: Capelson, M., Liang, Y., Schulte, R., Mair, W., Wagner, U., & Hetzer, M.
(2010). Chromatin-bound nuclear pore components regulate gene expression in higher
eukaryotes. Cell. Elsevier. https://doi.org/10.1016/j.cell.2009.12.054
chicago: Capelson, Maya, Yun Liang, Roberta Schulte, William Mair, Ulrich Wagner,
and Martin Hetzer. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression
in Higher Eukaryotes.” Cell. Elsevier, 2010. https://doi.org/10.1016/j.cell.2009.12.054.
ieee: M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, and M. Hetzer, “Chromatin-bound
nuclear pore components regulate gene expression in higher eukaryotes,” Cell,
vol. 140, no. 3. Elsevier, pp. 372–383, 2010.
ista: Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. 2010. Chromatin-bound
nuclear pore components regulate gene expression in higher eukaryotes. Cell. 140(3),
372–383.
mla: Capelson, Maya, et al. “Chromatin-Bound Nuclear Pore Components Regulate Gene
Expression in Higher Eukaryotes.” Cell, vol. 140, no. 3, Elsevier, 2010,
pp. 372–83, doi:10.1016/j.cell.2009.12.054.
short: M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140
(2010) 372–383.
date_created: 2022-04-07T07:53:36Z
date_published: 2010-02-05T00:00:00Z
date_updated: 2022-07-18T08:55:03Z
day: '05'
doi: 10.1016/j.cell.2009.12.054
extern: '1'
external_id:
pmid:
- '20144761'
intvolume: ' 140'
issue: '3'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2009.12.054
month: '02'
oa: 1
oa_version: Published Version
page: 372-383
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Chromatin-bound nuclear pore components regulate gene expression in higher
eukaryotes
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 140
year: '2010'
...
---
_id: '11103'
abstract:
- lang: eng
text: Over the last decade, the nuclear envelope (NE) has emerged as a key component
in the organization and function of the nuclear genome. As many as 100 different
proteins are thought to specifically localize to this double membrane that separates
the cytoplasm and the nucleoplasm of eukaryotic cells. Selective portals through
the NE are formed at sites where the inner and outer nuclear membranes are fused,
and the coincident assembly of ∼30 proteins into nuclear pore complexes occurs.
These nuclear pore complexes are essential for the control of nucleocytoplasmic
exchange. Many of the NE and nuclear pore proteins are thought to play crucial
roles in gene regulation and thus are increasingly linked to human diseases.
article_processing_charge: No
article_type: review
author:
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
- first_name: Susan R.
full_name: Wente, Susan R.
last_name: Wente
citation:
ama: 'Hetzer M, Wente SR. Border control at the nucleus: Biogenesis and organization
of the nuclear membrane and pore complexes. Developmental Cell. 2009;17(5):606-616.
doi:10.1016/j.devcel.2009.10.007'
apa: 'Hetzer, M., & Wente, S. R. (2009). Border control at the nucleus: Biogenesis
and organization of the nuclear membrane and pore complexes. Developmental
Cell. Elsevier. https://doi.org/10.1016/j.devcel.2009.10.007'
chicago: 'Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis
and Organization of the Nuclear Membrane and Pore Complexes.” Developmental
Cell. Elsevier, 2009. https://doi.org/10.1016/j.devcel.2009.10.007.'
ieee: 'M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and
organization of the nuclear membrane and pore complexes,” Developmental Cell,
vol. 17, no. 5. Elsevier, pp. 606–616, 2009.'
ista: 'Hetzer M, Wente SR. 2009. Border control at the nucleus: Biogenesis and organization
of the nuclear membrane and pore complexes. Developmental Cell. 17(5), 606–616.'
mla: 'Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis
and Organization of the Nuclear Membrane and Pore Complexes.” Developmental
Cell, vol. 17, no. 5, Elsevier, 2009, pp. 606–16, doi:10.1016/j.devcel.2009.10.007.'
short: M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.
date_created: 2022-04-07T07:53:45Z
date_published: 2009-11-17T00:00:00Z
date_updated: 2022-07-18T08:55:01Z
day: '17'
doi: 10.1016/j.devcel.2009.10.007
extern: '1'
external_id:
pmid:
- '19922866'
intvolume: ' 17'
issue: '5'
keyword:
- Developmental Biology
- Cell Biology
- General Biochemistry
- Genetics and Molecular Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.devcel.2009.10.007
month: '11'
oa: 1
oa_version: Published Version
page: 606-616
pmid: 1
publication: Developmental Cell
publication_identifier:
issn:
- 1534-5807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Border control at the nucleus: Biogenesis and organization of the nuclear
membrane and pore complexes'
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 17
year: '2009'
...
---
_id: '11105'
abstract:
- lang: eng
text: Nuclear-pore complexes (NPCs) are large protein channels that span the nuclear
envelope (NE), which is a double membrane that encloses the nuclear genome of
eukaryotes. Each of the typically 2,000–4,000 pores in the NE of vertebrate cells
is composed of multiple copies of 30 different proteins known as nucleoporins.
The evolutionarily conserved NPC proteins have the well-characterized function
of mediating the transport of molecules between the nucleoplasm and the cytoplasm.
Mutations in nucleoporins are often linked to specific developmental defects and
disease, and the resulting phenotypes are usually interpreted as the consequences
of perturbed nuclear transport activity. However, recent evidence suggests that
NPCs have additional functions in chromatin organization and gene regulation,
some of which might be independent of nuclear transport. Here, we review the transport-dependent
and transport-independent roles of NPCs in the regulation of nuclear function
and gene expression.
article_processing_charge: No
article_type: original
author:
- first_name: Maya
full_name: Capelson, Maya
last_name: Capelson
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Capelson M, Hetzer M. The role of nuclear pores in gene regulation, development
and disease. EMBO reports. 2009;10(7):697-705. doi:10.1038/embor.2009.147
apa: Capelson, M., & Hetzer, M. (2009). The role of nuclear pores in gene regulation,
development and disease. EMBO Reports. EMBO. https://doi.org/10.1038/embor.2009.147
chicago: Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation,
Development and Disease.” EMBO Reports. EMBO, 2009. https://doi.org/10.1038/embor.2009.147.
ieee: M. Capelson and M. Hetzer, “The role of nuclear pores in gene regulation,
development and disease,” EMBO reports, vol. 10, no. 7. EMBO, pp. 697–705,
2009.
ista: Capelson M, Hetzer M. 2009. The role of nuclear pores in gene regulation,
development and disease. EMBO reports. 10(7), 697–705.
mla: Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation,
Development and Disease.” EMBO Reports, vol. 10, no. 7, EMBO, 2009, pp.
697–705, doi:10.1038/embor.2009.147.
short: M. Capelson, M. Hetzer, EMBO Reports 10 (2009) 697–705.
date_created: 2022-04-07T07:54:06Z
date_published: 2009-07-01T00:00:00Z
date_updated: 2022-07-18T08:42:44Z
day: '01'
doi: 10.1038/embor.2009.147
extern: '1'
external_id:
pmid:
- '19543230'
intvolume: ' 10'
issue: '7'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/embor.2009.147
month: '07'
oa: 1
oa_version: Published Version
page: 697-705
pmid: 1
publication: EMBO reports
publication_identifier:
eissn:
- 1469-3178
issn:
- 1469-221X
publication_status: published
publisher: EMBO
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/embor.2009.176
scopus_import: '1'
status: public
title: The role of nuclear pores in gene regulation, development and disease
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 10
year: '2009'
...
---
_id: '11106'
abstract:
- lang: eng
text: Formation of the nuclear envelope (NE) around segregated chromosomes occurs
by the reshaping of the endoplasmic reticulum (ER), a reservoir for disassembled
nuclear membrane components during mitosis. In this study, we show that inner
nuclear membrane proteins such as lamin B receptor (LBR), MAN1, Lap2β, and the
trans-membrane nucleoporins Ndc1 and POM121 drive the spreading of ER membranes
into the emerging NE via their capacity to bind chromatin in a collaborative manner.
Despite their redundant functions, decreasing the levels of any of these trans-membrane
proteins by RNAi-mediated knockdown delayed NE formation, whereas increasing the
levels of any of them had the opposite effect. Furthermore, acceleration of NE
formation interferes with chromosome separation during mitosis, indicating that
the time frame over which chromatin becomes membrane enclosed is physiologically
relevant and regulated. These data suggest that functionally distinct classes
of chromatin-interacting membrane proteins, which are present at nonsaturating
levels, collaborate to rapidly reestablish the nuclear compartment at the end
of mitosis.
article_processing_charge: No
article_type: original
author:
- first_name: Daniel J.
full_name: Anderson, Daniel J.
last_name: Anderson
- first_name: Jesse D.
full_name: Vargas, Jesse D.
last_name: Vargas
- first_name: Joshua P.
full_name: Hsiao, Joshua P.
last_name: Hsiao
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. Recruitment of functionally distinct
membrane proteins to chromatin mediates nuclear envelope formation in vivo. Journal
of Cell Biology. 2009;186(2):183-191. doi:10.1083/jcb.200901106
apa: Anderson, D. J., Vargas, J. D., Hsiao, J. P., & Hetzer, M. (2009). Recruitment
of functionally distinct membrane proteins to chromatin mediates nuclear envelope
formation in vivo. Journal of Cell Biology. Rockefeller University Press.
https://doi.org/10.1083/jcb.200901106
chicago: Anderson, Daniel J., Jesse D. Vargas, Joshua P. Hsiao, and Martin Hetzer.
“Recruitment of Functionally Distinct Membrane Proteins to Chromatin Mediates
Nuclear Envelope Formation in Vivo.” Journal of Cell Biology. Rockefeller
University Press, 2009. https://doi.org/10.1083/jcb.200901106.
ieee: D. J. Anderson, J. D. Vargas, J. P. Hsiao, and M. Hetzer, “Recruitment of
functionally distinct membrane proteins to chromatin mediates nuclear envelope
formation in vivo,” Journal of Cell Biology, vol. 186, no. 2. Rockefeller
University Press, pp. 183–191, 2009.
ista: Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. 2009. Recruitment of functionally
distinct membrane proteins to chromatin mediates nuclear envelope formation in
vivo. Journal of Cell Biology. 186(2), 183–191.
mla: Anderson, Daniel J., et al. “Recruitment of Functionally Distinct Membrane
Proteins to Chromatin Mediates Nuclear Envelope Formation in Vivo.” Journal
of Cell Biology, vol. 186, no. 2, Rockefeller University Press, 2009, pp.
183–91, doi:10.1083/jcb.200901106.
short: D.J. Anderson, J.D. Vargas, J.P. Hsiao, M. Hetzer, Journal of Cell Biology
186 (2009) 183–191.
date_created: 2022-04-07T07:54:18Z
date_published: 2009-07-20T00:00:00Z
date_updated: 2022-07-18T08:58:35Z
day: '20'
doi: 10.1083/jcb.200901106
extern: '1'
external_id:
pmid:
- '19620630'
intvolume: ' 186'
issue: '2'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.200901106
month: '07'
oa: 1
oa_version: Published Version
page: 183-191
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1083/jcb.20090110620090903c
scopus_import: '1'
status: public
title: Recruitment of functionally distinct membrane proteins to chromatin mediates
nuclear envelope formation in vivo
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 186
year: '2009'
...
---
_id: '11107'
abstract:
- lang: eng
text: Nucleocytoplasmic transport occurs exclusively through nuclear pore complexes
(NPCs) embedded in pores formed by inner and outer nuclear membrane fusion. The
mechanism for de novo pore and NPC biogenesis remains unclear. Reticulons (RTNs)
and Yop1/DP1 are conserved membrane protein families required to form and maintain
the tubular endoplasmic reticulum (ER) and the postmitotic nuclear envelope. In
this study, we report that members of the RTN and Yop1/DP1 families are required
for nuclear pore formation. Analysis of Saccharomyces cerevisiae prp20-G282S and
nup133Δ NPC assembly mutants revealed perturbations in Rtn1–green fluorescent
protein (GFP) and Yop1-GFP ER distribution and colocalization to NPC clusters.
Combined deletion of RTN1 and YOP1 resulted in NPC clustering, nuclear import
defects, and synthetic lethality with the additional absence of Pom34, Pom152,
and Nup84 subcomplex members. We tested for a direct role in NPC biogenesis using
Xenopus laevis in vitro assays and found that anti-Rtn4a antibodies specifically
inhibited de novo nuclear pore formation. We hypothesize that these ER membrane–bending
proteins mediate early NPC assembly steps.
article_processing_charge: No
article_type: original
author:
- first_name: T. Renee
full_name: Dawson, T. Renee
last_name: Dawson
- first_name: Michelle D.
full_name: Lazarus, Michelle D.
last_name: Lazarus
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
- first_name: Susan R.
full_name: Wente, Susan R.
last_name: Wente
citation:
ama: Dawson TR, Lazarus MD, Hetzer M, Wente SR. ER membrane–bending proteins are
necessary for de novo nuclear pore formation. Journal of Cell Biology.
2009;184(5):659-675. doi:10.1083/jcb.200806174
apa: Dawson, T. R., Lazarus, M. D., Hetzer, M., & Wente, S. R. (2009). ER membrane–bending
proteins are necessary for de novo nuclear pore formation. Journal of Cell
Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.200806174
chicago: Dawson, T. Renee, Michelle D. Lazarus, Martin Hetzer, and Susan R. Wente.
“ER Membrane–Bending Proteins Are Necessary for de Novo Nuclear Pore Formation.”
Journal of Cell Biology. Rockefeller University Press, 2009. https://doi.org/10.1083/jcb.200806174.
ieee: T. R. Dawson, M. D. Lazarus, M. Hetzer, and S. R. Wente, “ER membrane–bending
proteins are necessary for de novo nuclear pore formation,” Journal of Cell
Biology, vol. 184, no. 5. Rockefeller University Press, pp. 659–675, 2009.
ista: Dawson TR, Lazarus MD, Hetzer M, Wente SR. 2009. ER membrane–bending proteins
are necessary for de novo nuclear pore formation. Journal of Cell Biology. 184(5),
659–675.
mla: Dawson, T. Renee, et al. “ER Membrane–Bending Proteins Are Necessary for de
Novo Nuclear Pore Formation.” Journal of Cell Biology, vol. 184, no. 5,
Rockefeller University Press, 2009, pp. 659–75, doi:10.1083/jcb.200806174.
short: T.R. Dawson, M.D. Lazarus, M. Hetzer, S.R. Wente, Journal of Cell Biology
184 (2009) 659–675.
date_created: 2022-04-07T07:54:44Z
date_published: 2009-03-09T00:00:00Z
date_updated: 2022-07-18T08:55:05Z
day: '09'
doi: 10.1083/jcb.200806174
extern: '1'
external_id:
pmid:
- '19273614'
intvolume: ' 184'
issue: '5'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.200806174
month: '03'
oa: 1
oa_version: Published Version
page: 659-675
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: ER membrane–bending proteins are necessary for de novo nuclear pore formation
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 184
year: '2009'
...
---
_id: '11108'
abstract:
- lang: eng
text: In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis
and reassemble into the newly forming nuclei. However, the fate of nuclear pores
in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear
structures, do not turn over in differentiated cells. While a subset of NPC components,
like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like
the Nup107/160 complex, are extremely long-lived and remain incorporated in the
nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin
expression and NPC turnover, we discovered an age-related deterioration of NPCs,
leading to an increase in nuclear permeability and the leaking of cytoplasmic
proteins into the nucleus. Our finding that nuclear “leakiness” is dramatically
accelerated during aging and that a subset of nucleoporins is oxidatively damaged
in old cells suggests that the accumulation of damage at the NPC might be a crucial
aging event.
article_processing_charge: No
article_type: original
author:
- first_name: Maximiliano A.
full_name: D'Angelo, Maximiliano A.
last_name: D'Angelo
- first_name: Marcela
full_name: Raices, Marcela
last_name: Raices
- first_name: Siler H.
full_name: Panowski, Siler H.
last_name: Panowski
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: D’Angelo MA, Raices M, Panowski SH, Hetzer M. Age-dependent deterioration of
nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells.
Cell. 2009;136(2):284-295. doi:10.1016/j.cell.2008.11.037
apa: D’Angelo, M. A., Raices, M., Panowski, S. H., & Hetzer, M. (2009). Age-dependent
deterioration of nuclear pore complexes causes a loss of nuclear integrity in
postmitotic cells. Cell. Elsevier. https://doi.org/10.1016/j.cell.2008.11.037
chicago: D’Angelo, Maximiliano A., Marcela Raices, Siler H. Panowski, and Martin
Hetzer. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of
Nuclear Integrity in Postmitotic Cells.” Cell. Elsevier, 2009. https://doi.org/10.1016/j.cell.2008.11.037.
ieee: M. A. D’Angelo, M. Raices, S. H. Panowski, and M. Hetzer, “Age-dependent deterioration
of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells,”
Cell, vol. 136, no. 2. Elsevier, pp. 284–295, 2009.
ista: D’Angelo MA, Raices M, Panowski SH, Hetzer M. 2009. Age-dependent deterioration
of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells.
Cell. 136(2), 284–295.
mla: D’Angelo, Maximiliano A., et al. “Age-Dependent Deterioration of Nuclear Pore
Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” Cell,
vol. 136, no. 2, Elsevier, 2009, pp. 284–95, doi:10.1016/j.cell.2008.11.037.
short: M.A. D’Angelo, M. Raices, S.H. Panowski, M. Hetzer, Cell 136 (2009) 284–295.
date_created: 2022-04-07T07:54:52Z
date_published: 2009-01-23T00:00:00Z
date_updated: 2022-07-18T08:55:29Z
day: '23'
doi: 10.1016/j.cell.2008.11.037
extern: '1'
external_id:
pmid:
- '19167330'
intvolume: ' 136'
issue: '2'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2008.11.037
month: '01'
oa: 1
oa_version: Published Version
page: 284-295
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear
integrity in postmitotic cells
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 136
year: '2009'
...
---
_id: '8480'
abstract:
- lang: eng
text: The KIX domain of the transcription co-activator CBP is a three-helix bundle
protein that folds via rapid accumulation of an intermediate state, followed by
a slower folding phase. Recent NMR relaxation dispersion studies revealed the
presence of a low-populated (excited) state of KIX that exists in equilibrium
with the natively folded form under non-denaturing conditions, and likely represents
the equilibrium analog of the folding intermediate. Here, we combine amide hydrogen/deuterium
exchange measurements using rapid NMR data acquisition techniques with backbone
15N and 13C relaxation dispersion experiments to further investigate the equilibrium
folding of the KIX domain. Residual structure within the folding intermediate
is detected by both methods, and their combination enables reliable quantification
of the amount of persistent residual structure. Three well-defined folding subunits
are found, which display variable stability and correspond closely to the individual
helices in the native state. While two of the three helices (α2 and α3) are partially
formed in the folding intermediate (to ∼ 50% and ∼ 80%, respectively, at 20 °C),
the third helix is disordered. The observed helical content within the excited
state exceeds the helical propensities predicted for the corresponding peptide
regions, suggesting that the two helices are weakly mutually stabilized, while
methyl 13C relaxation dispersion data indicate that a defined packing arrangement
is unlikely. Temperature-dependent experiments reveal that the largest enthalpy
and entropy changes along the folding reaction occur during the final transition
from the intermediate to the native state. Our experimental data are consistent
with a folding mechanism where helices α2 and α3 form rapidly, although to different
extents, while helix α1 consolidates only as folding proceeds to complete the
native state-structure.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Robert
full_name: Konrat, Robert
last_name: Konrat
- first_name: Martin
full_name: Tollinger, Martin
last_name: Tollinger
citation:
ama: 'Schanda P, Brutscher B, Konrat R, Tollinger M. Folding of the KIX domain:
Characterization of the equilibrium analog of a folding intermediate using 15N/13C
relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. Journal
of Molecular Biology. 2008;380(4):726-741. doi:10.1016/j.jmb.2008.05.040'
apa: 'Schanda, P., Brutscher, B., Konrat, R., & Tollinger, M. (2008). Folding
of the KIX domain: Characterization of the equilibrium analog of a folding intermediate
using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy.
Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2008.05.040'
chicago: 'Schanda, Paul, Bernhard Brutscher, Robert Konrat, and Martin Tollinger.
“Folding of the KIX Domain: Characterization of the Equilibrium Analog of a Folding
Intermediate Using 15N/13C Relaxation Dispersion and Fast 1H/2H Amide Exchange
NMR Spectroscopy.” Journal of Molecular Biology. Elsevier, 2008. https://doi.org/10.1016/j.jmb.2008.05.040.'
ieee: 'P. Schanda, B. Brutscher, R. Konrat, and M. Tollinger, “Folding of the KIX
domain: Characterization of the equilibrium analog of a folding intermediate using
15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy,”
Journal of Molecular Biology, vol. 380, no. 4. Elsevier, pp. 726–741, 2008.'
ista: 'Schanda P, Brutscher B, Konrat R, Tollinger M. 2008. Folding of the KIX domain:
Characterization of the equilibrium analog of a folding intermediate using 15N/13C
relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. Journal
of Molecular Biology. 380(4), 726–741.'
mla: 'Schanda, Paul, et al. “Folding of the KIX Domain: Characterization of the
Equilibrium Analog of a Folding Intermediate Using 15N/13C Relaxation Dispersion
and Fast 1H/2H Amide Exchange NMR Spectroscopy.” Journal of Molecular Biology,
vol. 380, no. 4, Elsevier, 2008, pp. 726–41, doi:10.1016/j.jmb.2008.05.040.'
short: P. Schanda, B. Brutscher, R. Konrat, M. Tollinger, Journal of Molecular Biology
380 (2008) 726–741.
date_created: 2020-09-18T10:12:29Z
date_published: 2008-07-18T00:00:00Z
date_updated: 2021-01-12T08:19:34Z
day: '18'
doi: 10.1016/j.jmb.2008.05.040
extern: '1'
intvolume: ' 380'
issue: '4'
keyword:
- Molecular Biology
language:
- iso: eng
month: '07'
oa_version: None
page: 726-741
publication: Journal of Molecular Biology
publication_identifier:
issn:
- 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Folding of the KIX domain: Characterization of the equilibrium analog of a
folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange
NMR spectroscopy'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 380
year: '2008'
...
---
_id: '8481'
abstract:
- lang: eng
text: 'The copK gene is localized on the pMOL30 plasmid of Cupriavidus metallidurans
CH34 within the complex cop cluster of genes, for which 21 genes have been identified.
The expression of the corresponding periplasmic CopK protein is strongly upregulated
in the presence of copper, leading to a high periplasmic accumulation. The structure
and metal-binding properties of CopK were investigated by NMR and mass spectrometry.
The protein is dimeric in the apo state with a dissociation constant in the range
of 10- 5 M estimated from analytical ultracentrifugation. Mass spectrometry revealed
that CopK has two high-affinity Cu(I)-binding sites per monomer with different
Cu(I) affinities. Binding of Cu(II) was observed but appeared to be non-specific.
The solution structure of apo-CopK revealed an all-β fold formed of two β-sheets
in perpendicular orientation with an unstructured C-terminal tail. The dimer interface
is formed by the surface of the C-terminal β-sheet. Binding of the first Cu(I)-ion
induces a major structural modification involving dissociation of the dimeric
apo-protein. Backbone chemical shifts determined for the 1Cu(I)-bound form confirm
the conservation of the N-terminal β-sheet, while the last strand of the C-terminal
sheet appears in slow conformational exchange. We hypothesize that the partial
disruption of the C-terminal β-sheet is related to dimer dissociation. NH-exchange
data acquired on the apo-protein are consistent with a lower thermodynamic stability
of the C-terminal sheet. CopK contains seven methionine residues, five of which
appear highly conserved. Chemical shift data suggest implication of two or three
methionines (Met54, Met38, Met28) in the first Cu(I) site. Addition of a second
Cu(I) ion further increases protein plasticity. Comparison of the structural and
metal-binding properties of CopK with other periplasmic copper-binding proteins
reveals two conserved features within these functionally related proteins: the
all-β fold and the methionine-rich Cu(I)-binding site.'
article_processing_charge: No
article_type: original
author:
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Sébastien
full_name: van Aelst, Sébastien
last_name: van Aelst
- first_name: Tatiana
full_name: Vallaeys, Tatiana
last_name: Vallaeys
- first_name: Jacques
full_name: Covès, Jacques
last_name: Covès
- first_name: Max
full_name: Mergeay, Max
last_name: Mergeay
- first_name: Ruddy
full_name: Wattiez, Ruddy
last_name: Wattiez
citation:
ama: Bersch B, Favier A, Schanda P, et al. Molecular structure and metal-binding
properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans
CH34 during copper challenge. Journal of Molecular Biology. 2008;380(2):386-403.
doi:10.1016/j.jmb.2008.05.017
apa: Bersch, B., Favier, A., Schanda, P., van Aelst, S., Vallaeys, T., Covès, J.,
… Wattiez, R. (2008). Molecular structure and metal-binding properties of the
periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper
challenge. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2008.05.017
chicago: Bersch, Beate, Adrien Favier, Paul Schanda, Sébastien van Aelst, Tatiana
Vallaeys, Jacques Covès, Max Mergeay, and Ruddy Wattiez. “Molecular Structure
and Metal-Binding Properties of the Periplasmic CopK Protein Expressed in Cupriavidus
Metallidurans CH34 during Copper Challenge.” Journal of Molecular Biology.
Elsevier, 2008. https://doi.org/10.1016/j.jmb.2008.05.017.
ieee: B. Bersch et al., “Molecular structure and metal-binding properties
of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during
copper challenge,” Journal of Molecular Biology, vol. 380, no. 2. Elsevier,
pp. 386–403, 2008.
ista: Bersch B, Favier A, Schanda P, van Aelst S, Vallaeys T, Covès J, Mergeay M,
Wattiez R. 2008. Molecular structure and metal-binding properties of the periplasmic
CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge.
Journal of Molecular Biology. 380(2), 386–403.
mla: Bersch, Beate, et al. “Molecular Structure and Metal-Binding Properties of
the Periplasmic CopK Protein Expressed in Cupriavidus Metallidurans CH34 during
Copper Challenge.” Journal of Molecular Biology, vol. 380, no. 2, Elsevier,
2008, pp. 386–403, doi:10.1016/j.jmb.2008.05.017.
short: B. Bersch, A. Favier, P. Schanda, S. van Aelst, T. Vallaeys, J. Covès, M.
Mergeay, R. Wattiez, Journal of Molecular Biology 380 (2008) 386–403.
date_created: 2020-09-18T10:12:37Z
date_published: 2008-07-04T00:00:00Z
date_updated: 2021-01-12T08:19:34Z
day: '04'
doi: 10.1016/j.jmb.2008.05.017
extern: '1'
intvolume: ' 380'
issue: '2'
keyword:
- Molecular Biology
language:
- iso: eng
month: '07'
oa_version: None
page: 386-403
publication: Journal of Molecular Biology
publication_identifier:
issn:
- 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Molecular structure and metal-binding properties of the periplasmic CopK protein
expressed in Cupriavidus metallidurans CH34 during copper challenge
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 380
year: '2008'
...
---
_id: '11109'
abstract:
- lang: eng
text: The nuclear envelope (NE) provides a selective barrier between the nuclear
interior and the cytoplasm and constitutes a central component of intracellular
architecture. During mitosis in metazoa, the NE breaks down leading to the complete
mixing of the nuclear content with the cytosol. Interestingly, many NE components
actively participate in mitotic progression. After chromosome segregation, the
NE is reassembled around decondensing chromatin and the nuclear compartment is
reestablished in the daughter cells. Here, we summarize recent progress in deciphering
the molecular mechanisms underlying NE dynamics during cell division.
article_processing_charge: No
article_type: original
author:
- first_name: Ulrike
full_name: Kutay, Ulrike
last_name: Kutay
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Kutay U, Hetzer M. Reorganization of the nuclear envelope during open mitosis.
Current Opinion in Cell Biology. 2008;20(6):669-677. doi:10.1016/j.ceb.2008.09.010
apa: Kutay, U., & Hetzer, M. (2008). Reorganization of the nuclear envelope
during open mitosis. Current Opinion in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2008.09.010
chicago: Kutay, Ulrike, and Martin Hetzer. “Reorganization of the Nuclear Envelope
during Open Mitosis.” Current Opinion in Cell Biology. Elsevier, 2008.
https://doi.org/10.1016/j.ceb.2008.09.010.
ieee: U. Kutay and M. Hetzer, “Reorganization of the nuclear envelope during open
mitosis,” Current Opinion in Cell Biology, vol. 20, no. 6. Elsevier, pp.
669–677, 2008.
ista: Kutay U, Hetzer M. 2008. Reorganization of the nuclear envelope during open
mitosis. Current Opinion in Cell Biology. 20(6), 669–677.
mla: Kutay, Ulrike, and Martin Hetzer. “Reorganization of the Nuclear Envelope during
Open Mitosis.” Current Opinion in Cell Biology, vol. 20, no. 6, Elsevier,
2008, pp. 669–77, doi:10.1016/j.ceb.2008.09.010.
short: U. Kutay, M. Hetzer, Current Opinion in Cell Biology 20 (2008) 669–677.
date_created: 2022-04-07T07:55:00Z
date_published: 2008-12-01T00:00:00Z
date_updated: 2022-07-18T08:55:32Z
day: '01'
doi: 10.1016/j.ceb.2008.09.010
extern: '1'
external_id:
pmid:
- '18938243'
intvolume: ' 20'
issue: '6'
keyword:
- Cell Biology
language:
- iso: eng
month: '12'
oa_version: None
page: 669-677
pmid: 1
publication: Current Opinion in Cell Biology
publication_identifier:
issn:
- 0955-0674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Reorganization of the nuclear envelope during open mitosis
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 20
year: '2008'
...
---
_id: '11110'
abstract:
- lang: eng
text: Nuclear pore complexes are large aqueous channels that penetrate the nuclear
envelope, thereby connecting the nuclear interior with the cytoplasm. Until recently,
these macromolecular complexes were viewed as static structures, the only function
of which was to control the molecular trafficking between the two compartments.
It has now become evident that this simplistic scenario is inaccurate and that
nuclear pore complexes are highly dynamic multiprotein assemblies involved in
diverse cellular processes ranging from the organization of the cytoskeleton to
gene expression. In this review, we discuss the most recent developments in the
nuclear-pore-complex field, focusing on the assembly, disassembly, maintenance
and function of this macromolecular structure.
article_processing_charge: No
article_type: review
author:
- first_name: Maximiliano A.
full_name: D’Angelo, Maximiliano A.
last_name: D’Angelo
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: D’Angelo MA, Hetzer M. Structure, dynamics and function of nuclear pore complexes.
Trends in Cell Biology. 2008;18(10):456-466. doi:10.1016/j.tcb.2008.07.009
apa: D’Angelo, M. A., & Hetzer, M. (2008). Structure, dynamics and function
of nuclear pore complexes. Trends in Cell Biology. Elsevier. https://doi.org/10.1016/j.tcb.2008.07.009
chicago: D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function
of Nuclear Pore Complexes.” Trends in Cell Biology. Elsevier, 2008. https://doi.org/10.1016/j.tcb.2008.07.009.
ieee: M. A. D’Angelo and M. Hetzer, “Structure, dynamics and function of nuclear
pore complexes,” Trends in Cell Biology, vol. 18, no. 10. Elsevier, pp.
456–466, 2008.
ista: D’Angelo MA, Hetzer M. 2008. Structure, dynamics and function of nuclear pore
complexes. Trends in Cell Biology. 18(10), 456–466.
mla: D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function
of Nuclear Pore Complexes.” Trends in Cell Biology, vol. 18, no. 10, Elsevier,
2008, pp. 456–66, doi:10.1016/j.tcb.2008.07.009.
short: M.A. D’Angelo, M. Hetzer, Trends in Cell Biology 18 (2008) 456–466.
date_created: 2022-04-07T07:55:10Z
date_published: 2008-10-01T00:00:00Z
date_updated: 2022-07-18T08:55:33Z
day: '01'
doi: 10.1016/j.tcb.2008.07.009
extern: '1'
external_id:
pmid:
- '18786826'
intvolume: ' 18'
issue: '10'
keyword:
- Cell Biology
language:
- iso: eng
month: '10'
oa_version: None
page: 456-466
pmid: 1
publication: Trends in Cell Biology
publication_identifier:
issn:
- 0962-8924
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure, dynamics and function of nuclear pore complexes
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 18
year: '2008'
...
---
_id: '11111'
abstract:
- lang: eng
text: During mitosis in metazoans, segregated chromosomes become enclosed by the
nuclear envelope (NE), a double membrane that is continuous with the endoplasmic
reticulum (ER). Recent in vitro data suggest that NE formation occurs by chromatin-mediated
reorganization of the tubular ER; however, the basic principles of such a membrane-reshaping
process remain uncharacterized. Here, we present a quantitative analysis of nuclear
membrane assembly in mammalian cells using time-lapse microscopy. From the initial
recruitment of ER tubules to chromatin, the formation of a membrane-enclosed,
transport-competent nucleus occurs within ∼12 min. Overexpression of the ER tubule-forming
proteins reticulon 3, reticulon 4, and DP1 inhibits NE formation and nuclear expansion,
whereas their knockdown accelerates nuclear assembly. This suggests that the transition
from membrane tubules to sheets is rate-limiting for nuclear assembly. Our results
provide evidence that ER-shaping proteins are directly involved in the reconstruction
of the nuclear compartment and that morphological restructuring of the ER is the
principal mechanism of NE formation in vivo.
article_processing_charge: No
article_type: original
author:
- first_name: Daniel J.
full_name: Anderson, Daniel J.
last_name: Anderson
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Anderson DJ, Hetzer M. Reshaping of the endoplasmic reticulum limits the rate
for nuclear envelope formation. Journal of Cell Biology. 2008;182(5):911-924.
doi:10.1083/jcb.200805140
apa: Anderson, D. J., & Hetzer, M. (2008). Reshaping of the endoplasmic reticulum
limits the rate for nuclear envelope formation. Journal of Cell Biology.
Rockefeller University Press. https://doi.org/10.1083/jcb.200805140
chicago: Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum
Limits the Rate for Nuclear Envelope Formation.” Journal of Cell Biology.
Rockefeller University Press, 2008. https://doi.org/10.1083/jcb.200805140.
ieee: D. J. Anderson and M. Hetzer, “Reshaping of the endoplasmic reticulum limits
the rate for nuclear envelope formation,” Journal of Cell Biology, vol.
182, no. 5. Rockefeller University Press, pp. 911–924, 2008.
ista: Anderson DJ, Hetzer M. 2008. Reshaping of the endoplasmic reticulum limits
the rate for nuclear envelope formation. Journal of Cell Biology. 182(5), 911–924.
mla: Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum
Limits the Rate for Nuclear Envelope Formation.” Journal of Cell Biology,
vol. 182, no. 5, Rockefeller University Press, 2008, pp. 911–24, doi:10.1083/jcb.200805140.
short: D.J. Anderson, M. Hetzer, Journal of Cell Biology 182 (2008) 911–924.
date_created: 2022-04-07T07:55:23Z
date_published: 2008-09-08T00:00:00Z
date_updated: 2022-07-18T08:56:02Z
day: '08'
doi: 10.1083/jcb.200805140
extern: '1'
external_id:
pmid:
- '18779370'
intvolume: ' 182'
issue: '5'
keyword:
- Cell Biology
language:
- iso: eng
month: '09'
oa_version: None
page: 911-924
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope
formation
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 182
year: '2008'
...
---
_id: '11112'
abstract:
- lang: eng
text: The nuclear envelope is a double-layered membrane that encloses the nuclear
genome and transcriptional machinery. In dividing cells of metazoa, the nucleus
completely disassembles during mitosis, creating the need to re-establish the
nuclear compartment at the end of each cell division. Given the crucial role of
the nuclear envelope in gene regulation and cellular organization, it is not surprising
that its biogenesis and organization have become active research areas. We will
review recent insights into nuclear membrane dynamics during the cell cycle.
article_processing_charge: No
article_type: original
author:
- first_name: Daniel J
full_name: Anderson, Daniel J
last_name: Anderson
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Anderson DJ, Hetzer M. The life cycle of the metazoan nuclear envelope. Current
Opinion in Cell Biology. 2008;20(4):386-392. doi:10.1016/j.ceb.2008.03.016
apa: Anderson, D. J., & Hetzer, M. (2008). The life cycle of the metazoan nuclear
envelope. Current Opinion in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2008.03.016
chicago: Anderson, Daniel J, and Martin Hetzer. “The Life Cycle of the Metazoan
Nuclear Envelope.” Current Opinion in Cell Biology. Elsevier, 2008. https://doi.org/10.1016/j.ceb.2008.03.016.
ieee: D. J. Anderson and M. Hetzer, “The life cycle of the metazoan nuclear envelope,”
Current Opinion in Cell Biology, vol. 20, no. 4. Elsevier, pp. 386–392,
2008.
ista: Anderson DJ, Hetzer M. 2008. The life cycle of the metazoan nuclear envelope.
Current Opinion in Cell Biology. 20(4), 386–392.
mla: Anderson, Daniel J., and Martin Hetzer. “The Life Cycle of the Metazoan Nuclear
Envelope.” Current Opinion in Cell Biology, vol. 20, no. 4, Elsevier, 2008,
pp. 386–92, doi:10.1016/j.ceb.2008.03.016.
short: D.J. Anderson, M. Hetzer, Current Opinion in Cell Biology 20 (2008) 386–392.
date_created: 2022-04-07T07:55:34Z
date_published: 2008-08-01T00:00:00Z
date_updated: 2022-07-18T08:56:07Z
day: '01'
doi: 10.1016/j.ceb.2008.03.016
extern: '1'
external_id:
pmid:
- '18495454'
intvolume: ' 20'
issue: '4'
keyword:
- Cell Biology
language:
- iso: eng
month: '08'
oa_version: None
page: 386-392
pmid: 1
publication: Current Opinion in Cell Biology
publication_identifier:
issn:
- 0955-0674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: The life cycle of the metazoan nuclear envelope
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 20
year: '2008'
...
---
_id: '11113'
abstract:
- lang: eng
text: The nuclear envelope (NE), a double membrane enclosing the nucleus of eukaryotic
cells, controls the flow of information between the nucleoplasm and the cytoplasm
and provides a scaffold for the organization of chromatin and the cytoskeleton.
In dividing metazoan cells, the NE breaks down at the onset of mitosis and then
reforms around segregated chromosomes to generate the daughter nuclei. Recent
data from intact cells and cell-free nuclear assembly systems suggest that the
endoplasmic reticulum (ER) is the source of membrane for NE assembly. At the end
of mitosis, ER membrane tubules are targeted to chromatin via tubule ends and
reorganized into flat nuclear membrane sheets by specific DNA-binding membrane
proteins. In contrast to previous models, which proposed vesicle fusion to be
the principal mechanism of NE formation, these new studies suggest that the nuclear
membrane forms by the chromatin-mediated reshaping of the ER.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Daniel J.
full_name: Anderson, Daniel J.
last_name: Anderson
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Anderson DJ, Hetzer M. Shaping the endoplasmic reticulum into the nuclear envelope.
Journal of Cell Science. 2008;121(2):137-142. doi:10.1242/jcs.005777
apa: Anderson, D. J., & Hetzer, M. (2008). Shaping the endoplasmic reticulum
into the nuclear envelope. Journal of Cell Science. The Company of Biologists.
https://doi.org/10.1242/jcs.005777
chicago: Anderson, Daniel J., and Martin Hetzer. “Shaping the Endoplasmic Reticulum
into the Nuclear Envelope.” Journal of Cell Science. The Company of Biologists,
2008. https://doi.org/10.1242/jcs.005777.
ieee: D. J. Anderson and M. Hetzer, “Shaping the endoplasmic reticulum into the
nuclear envelope,” Journal of Cell Science, vol. 121, no. 2. The Company
of Biologists, pp. 137–142, 2008.
ista: Anderson DJ, Hetzer M. 2008. Shaping the endoplasmic reticulum into the nuclear
envelope. Journal of Cell Science. 121(2), 137–142.
mla: Anderson, Daniel J., and Martin Hetzer. “Shaping the Endoplasmic Reticulum
into the Nuclear Envelope.” Journal of Cell Science, vol. 121, no. 2, The
Company of Biologists, 2008, pp. 137–42, doi:10.1242/jcs.005777.
short: D.J. Anderson, M. Hetzer, Journal of Cell Science 121 (2008) 137–142.
date_created: 2022-04-07T07:55:46Z
date_published: 2008-01-15T00:00:00Z
date_updated: 2022-07-18T08:56:10Z
day: '15'
doi: 10.1242/jcs.005777
extern: '1'
external_id:
pmid:
- '18187447'
intvolume: ' 121'
issue: '2'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1242/jcs.005777
month: '01'
oa: 1
oa_version: Published Version
page: 137-142
pmid: 1
publication: Journal of Cell Science
publication_identifier:
eissn:
- 1477-9137
issn:
- 0021-9533
publication_status: published
publisher: The Company of Biologists
quality_controlled: '1'
scopus_import: '1'
status: public
title: Shaping the endoplasmic reticulum into the nuclear envelope
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 121
year: '2008'
...
---
_id: '11115'
abstract:
- lang: eng
text: The formation of the nuclear envelope (NE) around chromatin is a major membrane-remodelling
event that occurs during cell division of metazoa. It is unclear whether the nuclear
membrane reforms by the fusion of NE fragments or if it re-emerges from an intact
tubular network of the endoplasmic reticulum (ER). Here, we show that NE formation
and expansion requires a tubular ER network and occurs efficiently in the presence
of the membrane fusion inhibitor GTPγS. Chromatin recruitment of membranes, which
is initiated by tubule-end binding, followed by the formation, expansion and sealing
of flat membrane sheets, is mediated by DNA-binding proteins residing in the ER.
Thus, chromatin plays an active role in reshaping of the ER during NE formation.
article_processing_charge: No
article_type: original
author:
- first_name: Daniel J.
full_name: Anderson, Daniel J.
last_name: Anderson
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Anderson DJ, Hetzer M. Nuclear envelope formation by chromatin-mediated reorganization
of the endoplasmic reticulum. Nature Cell Biology. 2007;9(10):1160-1166.
doi:10.1038/ncb1636
apa: Anderson, D. J., & Hetzer, M. (2007). Nuclear envelope formation by chromatin-mediated
reorganization of the endoplasmic reticulum. Nature Cell Biology. Springer
Nature. https://doi.org/10.1038/ncb1636
chicago: Anderson, Daniel J., and Martin Hetzer. “Nuclear Envelope Formation by
Chromatin-Mediated Reorganization of the Endoplasmic Reticulum.” Nature Cell
Biology. Springer Nature, 2007. https://doi.org/10.1038/ncb1636.
ieee: D. J. Anderson and M. Hetzer, “Nuclear envelope formation by chromatin-mediated
reorganization of the endoplasmic reticulum,” Nature Cell Biology, vol.
9, no. 10. Springer Nature, pp. 1160–1166, 2007.
ista: Anderson DJ, Hetzer M. 2007. Nuclear envelope formation by chromatin-mediated
reorganization of the endoplasmic reticulum. Nature Cell Biology. 9(10), 1160–1166.
mla: Anderson, Daniel J., and Martin Hetzer. “Nuclear Envelope Formation by Chromatin-Mediated
Reorganization of the Endoplasmic Reticulum.” Nature Cell Biology, vol.
9, no. 10, Springer Nature, 2007, pp. 1160–66, doi:10.1038/ncb1636.
short: D.J. Anderson, M. Hetzer, Nature Cell Biology 9 (2007) 1160–1166.
date_created: 2022-04-07T07:56:04Z
date_published: 2007-09-09T00:00:00Z
date_updated: 2022-07-18T08:56:38Z
day: '09'
doi: 10.1038/ncb1636
extern: '1'
external_id:
pmid:
- '17828249'
intvolume: ' 9'
issue: '10'
keyword:
- Cell Biology
language:
- iso: eng
month: '09'
oa_version: None
page: 1160-1166
pmid: 1
publication: Nature Cell Biology
publication_identifier:
eissn:
- 1476-4679
issn:
- 1465-7392
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic
reticulum
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 9
year: '2007'
...