---
_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: '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: '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: '12200'
abstract:
- lang: eng
text: Key steps in the evolution of the angiosperm anther include the patterning
of the concentrically organized microsporangium and the incorporation of four
such microsporangia into a leaf-like structure. Mutant studies in the model plant
Arabidopsis thaliana are leading to an increasingly accurate picture of (i) the
cell lineages culminating in the different cell types present in the microsporangium
(the microsporocytes, the tapetum, and the middle and endothecial layers), and
(ii) some of the genes responsible for specifying their fates. However, the processes
that confer polarity on the developing anther and position the microsporangia
within it remain unclear. Certainly, data from a range of experimental strategies
suggest that hormones play a central role in establishing polarity and the patterning
of the anther initial, and may be responsible for locating the microsporangia.
But the fact that microsporangia were originally positioned externally suggests
that their development is likely to be autonomous, perhaps with the reproductive
cells generating signals controlling the growth and division of the investing
anther epidermis. These possibilities are discussed in the context of the expression
of genes which initiate and maintain male and female reproductive development,
and in the perspective of our current views of anther evolution.
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. Cell–cell interactions during patterning of the Arabidopsis
anther. Biochemical Society Transactions. 2010;38(2):571-576. doi:10.1042/bst0380571
apa: Feng, X., & Dickinson, H. G. (2010). Cell–cell interactions during patterning
of the Arabidopsis anther. Biochemical Society Transactions. Portland
Press Ltd. https://doi.org/10.1042/bst0380571
chicago: Feng, Xiaoqi, and Hugh G. Dickinson. “Cell–Cell Interactions during Patterning
of the Arabidopsis Anther.” Biochemical Society Transactions. Portland
Press Ltd., 2010. https://doi.org/10.1042/bst0380571.
ieee: X. Feng and H. G. Dickinson, “Cell–cell interactions during patterning of
the Arabidopsis anther,” Biochemical Society Transactions, vol.
38, no. 2. Portland Press Ltd., pp. 571–576, 2010.
ista: Feng X, Dickinson HG. 2010. Cell–cell interactions during patterning of the
Arabidopsis anther. Biochemical Society Transactions. 38(2), 571–576.
mla: Feng, Xiaoqi, and Hugh G. Dickinson. “Cell–Cell Interactions during Patterning
of the Arabidopsis Anther.” Biochemical Society Transactions, vol.
38, no. 2, Portland Press Ltd., 2010, pp. 571–76, doi:10.1042/bst0380571.
short: X. Feng, H.G. Dickinson, Biochemical Society Transactions 38 (2010) 571–576.
date_created: 2023-01-16T09:22:18Z
date_published: 2010-03-22T00:00:00Z
date_updated: 2023-05-08T10:57:59Z
day: '22'
department:
- _id: XiFe
doi: 10.1042/bst0380571
extern: '1'
external_id:
pmid:
- '20298223'
intvolume: ' 38'
issue: '2'
keyword:
- Biochemistry
- Anther Development
- Arabidopsis
- Cell Fate
- Microsporangium
- Polarity
- Receptor Kinase
language:
- iso: eng
month: '03'
oa_version: None
page: 571-576
pmid: 1
publication: Biochemical Society Transactions
publication_identifier:
issn:
- 0300-5127
- 1470-8752
publication_status: published
publisher: Portland Press Ltd.
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cell–cell interactions during patterning of the Arabidopsis anther
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 38
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: '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: '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'
...
---
_id: '11117'
abstract:
- lang: eng
text: Over the last years it has become evident that the nuclear envelope (NE) is
more than a passive membrane barrier that separates the nucleus from the cytoplasm.
The NE not only controls the trafficking of macromolecules between the nucleoplasm
and the cytosol, but also provides anchoring sites for chromosomes and cytoskeleton
to the nuclear periphery. Targeting of chromatin to the NE might actually be part
of gene expression regulation in eukaryotes. Mutations in certain NE proteins
are associated with a diversity of human diseases, including muscular dystrophy,
neuropathy, lipodistrophy, torsion dystonia and the premature aging condition
progeria. Despite the importance of the NE for cell division and differentiation,
relatively little is known about its biogenesis and its role in human diseases.
It is our goal to provide a comprehensive view of the NE and to discuss possible
implications of NE-associated changes for gene expression, chromatin organization
and signal transduction.
article_processing_charge: No
article_type: review
author:
- first_name: M. A.
full_name: D’Angelo, M. 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. The role of the nuclear envelope in cellular organization.
Cellular and Molecular Life Sciences. 2006;63(3):316-332. doi:10.1007/s00018-005-5361-3
apa: D’Angelo, M. A., & Hetzer, M. (2006). The role of the nuclear envelope
in cellular organization. Cellular and Molecular Life Sciences. Springer
Nature. https://doi.org/10.1007/s00018-005-5361-3
chicago: D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in
Cellular Organization.” Cellular and Molecular Life Sciences. Springer
Nature, 2006. https://doi.org/10.1007/s00018-005-5361-3.
ieee: M. A. D’Angelo and M. Hetzer, “The role of the nuclear envelope in cellular
organization,” Cellular and Molecular Life Sciences, vol. 63, no. 3. Springer
Nature, pp. 316–332, 2006.
ista: D’Angelo MA, Hetzer M. 2006. The role of the nuclear envelope in cellular
organization. Cellular and Molecular Life Sciences. 63(3), 316–332.
mla: D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in Cellular
Organization.” Cellular and Molecular Life Sciences, vol. 63, no. 3, Springer
Nature, 2006, pp. 316–32, doi:10.1007/s00018-005-5361-3.
short: M.A. D’Angelo, M. Hetzer, Cellular and Molecular Life Sciences 63 (2006)
316–332.
date_created: 2022-04-07T07:56:22Z
date_published: 2006-01-02T00:00:00Z
date_updated: 2022-07-18T08:56:58Z
day: '02'
doi: 10.1007/s00018-005-5361-3
extern: '1'
external_id:
pmid:
- '16389459'
intvolume: ' 63'
issue: '3'
keyword:
- Cell Biology
- Cellular and Molecular Neuroscience
- Pharmacology
- Molecular Biology
- Molecular Medicine
language:
- iso: eng
month: '01'
oa_version: None
page: 316-332
pmid: 1
publication: Cellular and Molecular Life Sciences
publication_identifier:
eissn:
- 1420-9071
issn:
- 1420-682X
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: The role of the nuclear envelope in cellular organization
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 63
year: '2006'
...
---
_id: '11120'
abstract:
- lang: eng
text: The nuclear envelope (NE) is a highly specialized membrane that delineates
the eukaryotic cell nucleus. It is composed of the inner and outer nuclear membranes,
nuclear pore complexes (NPCs) and, in metazoa, the lamina. The NE not only regulates
the trafficking of macromolecules between nucleoplasm and cytosol but also provides
anchoring sites for chromatin and the cytoskeleton. Through these interactions,
the NE helps position the nucleus within the cell and chromosomes within the nucleus,
thereby regulating the expression of certain genes. The NE is not static, rather
it is continuously remodeled during cell division. The most dramatic example of
NE reorganization occurs during mitosis in metazoa when the NE undergoes a complete
cycle of disassembly and reformation. Despite the importance of the NE for eukaryotic
cell life, relatively little is known about its biogenesis or many of its functions.
We thus are far from understanding the molecular etiology of a diverse group of
NE-associated diseases.
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
- first_name: Tobias C.
full_name: Walther, Tobias C.
last_name: Walther
- first_name: Iain W.
full_name: Mattaj, Iain W.
last_name: Mattaj
citation:
ama: 'Hetzer M, Walther TC, Mattaj IW. Pushing the envelope: Structure, function,
and dynamics of the nuclear periphery. Annual Review of Cell and Developmental
Biology. 2005;21:347-380. doi:10.1146/annurev.cellbio.21.090704.151152'
apa: 'Hetzer, M., Walther, T. C., & Mattaj, I. W. (2005). Pushing the envelope:
Structure, function, and dynamics of the nuclear periphery. Annual Review of
Cell and Developmental Biology. Annual Reviews. https://doi.org/10.1146/annurev.cellbio.21.090704.151152'
chicago: 'Hetzer, Martin, Tobias C. Walther, and Iain W. Mattaj. “Pushing the Envelope:
Structure, Function, and Dynamics of the Nuclear Periphery.” Annual Review
of Cell and Developmental Biology. Annual Reviews, 2005. https://doi.org/10.1146/annurev.cellbio.21.090704.151152.'
ieee: 'M. Hetzer, T. C. Walther, and I. W. Mattaj, “Pushing the envelope: Structure,
function, and dynamics of the nuclear periphery,” Annual Review of Cell and
Developmental Biology, vol. 21. Annual Reviews, pp. 347–380, 2005.'
ista: 'Hetzer M, Walther TC, Mattaj IW. 2005. Pushing the envelope: Structure, function,
and dynamics of the nuclear periphery. Annual Review of Cell and Developmental
Biology. 21, 347–380.'
mla: 'Hetzer, Martin, et al. “Pushing the Envelope: Structure, Function, and Dynamics
of the Nuclear Periphery.” Annual Review of Cell and Developmental Biology,
vol. 21, Annual Reviews, 2005, pp. 347–80, doi:10.1146/annurev.cellbio.21.090704.151152.'
short: M. Hetzer, T.C. Walther, I.W. Mattaj, Annual Review of Cell and Developmental
Biology 21 (2005) 347–380.
date_created: 2022-04-07T07:56:52Z
date_published: 2005-11-10T00:00:00Z
date_updated: 2022-07-18T08:57:34Z
day: '10'
doi: 10.1146/annurev.cellbio.21.090704.151152
extern: '1'
external_id:
pmid:
- '16212499'
intvolume: ' 21'
keyword:
- Cell Biology
- Developmental Biology
language:
- iso: eng
month: '11'
oa_version: None
page: 347-380
pmid: 1
publication: Annual Review of Cell and Developmental Biology
publication_identifier:
eissn:
- 1530-8995
issn:
- 1081-0706
publication_status: published
publisher: Annual Reviews
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Pushing the envelope: Structure, function, and dynamics of the nuclear periphery'
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 21
year: '2005'
...
---
_id: '11123'
abstract:
- lang: eng
text: The small GTPase Ran is a key regulator of nucleocytoplasmic transport during
interphase. The asymmetric distribution of the GTP-bound form of Ran across the
nuclear envelope — that is, large quantities in the nucleus compared with small
quantities in the cytoplasm — determines the directionality of many nuclear transport
processes. Recent findings that Ran also functions in spindle formation and nuclear
envelope assembly during mitosis suggest that Ran has a general role in chromatin-centred
processes. Ran functions in these events as a signal for chromosome position.
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
- first_name: Oliver J.
full_name: Gruss, Oliver J.
last_name: Gruss
- first_name: Iain W.
full_name: Mattaj, Iain W.
last_name: Mattaj
citation:
ama: Hetzer M, Gruss OJ, Mattaj IW. The Ran GTPase as a marker of chromosome position
in spindle formation and nuclear envelope assembly. Nature Cell Biology.
2002;4(7):E177-E184. doi:10.1038/ncb0702-e177
apa: Hetzer, M., Gruss, O. J., & Mattaj, I. W. (2002). The Ran GTPase as a marker
of chromosome position in spindle formation and nuclear envelope assembly. Nature
Cell Biology. Springer Nature. https://doi.org/10.1038/ncb0702-e177
chicago: Hetzer, Martin, Oliver J. Gruss, and Iain W. Mattaj. “The Ran GTPase as
a Marker of Chromosome Position in Spindle Formation and Nuclear Envelope Assembly.”
Nature Cell Biology. Springer Nature, 2002. https://doi.org/10.1038/ncb0702-e177.
ieee: M. Hetzer, O. J. Gruss, and I. W. Mattaj, “The Ran GTPase as a marker of chromosome
position in spindle formation and nuclear envelope assembly,” Nature Cell Biology,
vol. 4, no. 7. Springer Nature, pp. E177–E184, 2002.
ista: Hetzer M, Gruss OJ, Mattaj IW. 2002. The Ran GTPase as a marker of chromosome
position in spindle formation and nuclear envelope assembly. Nature Cell Biology.
4(7), E177–E184.
mla: Hetzer, Martin, et al. “The Ran GTPase as a Marker of Chromosome Position in
Spindle Formation and Nuclear Envelope Assembly.” Nature Cell Biology,
vol. 4, no. 7, Springer Nature, 2002, pp. E177–84, doi:10.1038/ncb0702-e177.
short: M. Hetzer, O.J. Gruss, I.W. Mattaj, Nature Cell Biology 4 (2002) E177–E184.
date_created: 2022-04-07T07:57:19Z
date_published: 2002-07-01T00:00:00Z
date_updated: 2022-07-18T08:58:03Z
day: '01'
doi: 10.1038/ncb0702-e177
extern: '1'
external_id:
pmid:
- '12105431'
intvolume: ' 4'
issue: '7'
keyword:
- Cell Biology
language:
- iso: eng
month: '07'
oa_version: None
page: E177-E184
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: The Ran GTPase as a marker of chromosome position in spindle formation and
nuclear envelope assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 4
year: '2002'
...
---
_id: '13438'
abstract:
- lang: eng
text: ICln is an ion channel identified by expression cloning using a cDNA library
from Madin-Darby canine kidney cells. In all organisms tested so far, only one
transcript for the ICln protein could be identified. Here we show that two splice
variants of the ICln ion channel can be found in Caenorhabditis elegans. Moreover,
we show that these two splice variants of the ICln channel protein, which we termed
IClnN1 and IClnN2, can be functionally reconstituted and tested in an artificial
lipid bilayer. In these experiments, the IClnN1-induced currents showed no voltage-dependent
inactivation, whereas the IClnN2-induced currents fully inactivated at positive
potentials. The molecular entity responsible for the voltage-dependent inactivation
of IClnN2 is a cluster of positively charged amino acids encoded by exon 2a, which
is absent in IClnN1. Our experiments suggest a mechanism of channel inactivation
that is similar to the “ball and chain” model proposed for the Shaker potassium
channel,i.e. a cluster of positively charged amino acids hinders ion permeation
through the channel by a molecular and voltage-dependent interaction at the inner
vestibulum of the pore. This hypothesis is supported by the finding that synthetic
peptides with the same amino acid sequence as the positive cluster can transform
the IClnN1-induced current to the current observed after reconstitution of IClnN2.
Furthermore, we show that the nematode ICln gene is embedded in an operon harboring
two additional genes, which we termed Nx and Ny. Co-reconstitution of Nx and IClnN2
and functional analysis of the related currents revealed a functional interaction
between the two proteins, as evidenced by the fact that the IClnN2-induced current
in the presence of Nx was no longer voltage-sensitive. The experiments described
indicate that the genome organization in nematodes allows an effective approach
for the identification of functional partner proteins of ion channels.
acknowledgement: We are grateful to D. E. Clapham, E. Wöll, G. Meyer, and G. Botta
for helpful discussion and/or reading of the manuscript. We also thank T. Stiernagle
for providing the N2 strain of C. elegans and A. Wimmer and M. Frick for technical
assistance
article_processing_charge: No
article_type: original
author:
- first_name: Johannes
full_name: Fürst, Johannes
last_name: Fürst
- first_name: Markus
full_name: Ritter, Markus
last_name: Ritter
- first_name: Jakob
full_name: Rudzki, Jakob
last_name: Rudzki
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
- first_name: Martin
full_name: Gschwentner, Martin
last_name: Gschwentner
- first_name: Elke
full_name: Scandella, Elke
last_name: Scandella
- first_name: Martin
full_name: Jakab, Martin
last_name: Jakab
- first_name: Matthias
full_name: König, Matthias
last_name: König
- first_name: Bernhard
full_name: Oehl, Bernhard
last_name: Oehl
- first_name: Florian
full_name: Lang, Florian
last_name: Lang
- first_name: Peter
full_name: Deetjen, Peter
last_name: Deetjen
- first_name: Markus
full_name: Paulmichl, Markus
last_name: Paulmichl
citation:
ama: Fürst J, Ritter M, Rudzki J, et al. ICln Ion channel splice variants in Caenorhabditis
elegans. Journal of Biological Chemistry. 2002;277(6):4435-4445. doi:10.1074/jbc.m107372200
apa: Fürst, J., Ritter, M., Rudzki, J., Danzl, J. G., Gschwentner, M., Scandella,
E., … Paulmichl, M. (2002). ICln Ion channel splice variants in Caenorhabditis
elegans. Journal of Biological Chemistry. Elsevier. https://doi.org/10.1074/jbc.m107372200
chicago: Fürst, Johannes, Markus Ritter, Jakob Rudzki, Johann G Danzl, Martin Gschwentner,
Elke Scandella, Martin Jakab, et al. “ICln Ion Channel Splice Variants in Caenorhabditis
Elegans.” Journal of Biological Chemistry. Elsevier, 2002. https://doi.org/10.1074/jbc.m107372200.
ieee: J. Fürst et al., “ICln Ion channel splice variants in Caenorhabditis
elegans,” Journal of Biological Chemistry, vol. 277, no. 6. Elsevier, pp.
4435–4445, 2002.
ista: Fürst J, Ritter M, Rudzki J, Danzl JG, Gschwentner M, Scandella E, Jakab M,
König M, Oehl B, Lang F, Deetjen P, Paulmichl M. 2002. ICln Ion channel splice
variants in Caenorhabditis elegans. Journal of Biological Chemistry. 277(6), 4435–4445.
mla: Fürst, Johannes, et al. “ICln Ion Channel Splice Variants in Caenorhabditis
Elegans.” Journal of Biological Chemistry, vol. 277, no. 6, Elsevier, 2002,
pp. 4435–45, doi:10.1074/jbc.m107372200.
short: J. Fürst, M. Ritter, J. Rudzki, J.G. Danzl, M. Gschwentner, E. Scandella,
M. Jakab, M. König, B. Oehl, F. Lang, P. Deetjen, M. Paulmichl, Journal of Biological
Chemistry 277 (2002) 4435–4445.
date_created: 2023-08-01T12:37:50Z
date_published: 2002-02-08T00:00:00Z
date_updated: 2023-08-01T12:55:54Z
day: '08'
ddc:
- '570'
doi: 10.1074/jbc.m107372200
extern: '1'
external_id:
pmid:
- '11706026'
file:
- access_level: open_access
checksum: 13abe20f78eb37ab62beb006f62c69b7
content_type: application/pdf
creator: alisjak
date_created: 2023-08-01T12:44:09Z
date_updated: 2023-08-01T12:44:09Z
file_id: '13439'
file_name: 2002_JBC_Fuerst.pdf
file_size: 798920
relation: main_file
success: 1
file_date_updated: 2023-08-01T12:44:09Z
has_accepted_license: '1'
intvolume: ' 277'
issue: '6'
keyword:
- Cell Biology
- Molecular Biology
- Biochemistry
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: 4435-4445
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
issn:
- 0021-9258
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: ICln Ion channel splice variants in Caenorhabditis elegans
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 277
year: '2002'
...
---
_id: '11125'
abstract:
- lang: eng
text: Although nuclear envelope (NE) assembly is known to require the GTPase Ran,
the membrane fusion machinery involved is uncharacterized. NE assembly involves
formation of a reticular network on chromatin, fusion of this network into a closed
NE and subsequent expansion. Here we show that p97, an AAA-ATPase previously implicated
in fusion of Golgi and transitional endoplasmic reticulum (ER) membranes together
with the adaptor p47, has two discrete functions in NE assembly. Formation of
a closed NE requires the p97–Ufd1–Npl4 complex, not previously implicated in membrane
fusion. Subsequent NE growth involves a p97–p47 complex. This study provides the
first insights into the molecular mechanisms and specificity of fusion events
involved in NE formation.
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
- first_name: Hemmo H.
full_name: Meyer, Hemmo H.
last_name: Meyer
- first_name: Tobias C.
full_name: Walther, Tobias C.
last_name: Walther
- first_name: Daniel
full_name: Bilbao-Cortes, Daniel
last_name: Bilbao-Cortes
- first_name: Graham
full_name: Warren, Graham
last_name: Warren
- first_name: Iain W.
full_name: Mattaj, Iain W.
last_name: Mattaj
citation:
ama: Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. Distinct
AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nature
Cell Biology. 2001;3(12):1086-1091. doi:10.1038/ncb1201-1086
apa: Hetzer, M., Meyer, H. H., Walther, T. C., Bilbao-Cortes, D., Warren, G., &
Mattaj, I. W. (2001). Distinct AAA-ATPase p97 complexes function in discrete steps
of nuclear assembly. Nature Cell Biology. Springer Nature. https://doi.org/10.1038/ncb1201-1086
chicago: Hetzer, Martin, Hemmo H. Meyer, Tobias C. Walther, Daniel Bilbao-Cortes,
Graham Warren, and Iain W. Mattaj. “Distinct AAA-ATPase P97 Complexes Function
in Discrete Steps of Nuclear Assembly.” Nature Cell Biology. Springer Nature,
2001. https://doi.org/10.1038/ncb1201-1086.
ieee: M. Hetzer, H. H. Meyer, T. C. Walther, D. Bilbao-Cortes, G. Warren, and I.
W. Mattaj, “Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear
assembly,” Nature Cell Biology, vol. 3, no. 12. Springer Nature, pp. 1086–1091,
2001.
ista: Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. 2001.
Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly.
Nature Cell Biology. 3(12), 1086–1091.
mla: Hetzer, Martin, et al. “Distinct AAA-ATPase P97 Complexes Function in Discrete
Steps of Nuclear Assembly.” Nature Cell Biology, vol. 3, no. 12, Springer
Nature, 2001, pp. 1086–91, doi:10.1038/ncb1201-1086.
short: M. Hetzer, H.H. Meyer, T.C. Walther, D. Bilbao-Cortes, G. Warren, I.W. Mattaj,
Nature Cell Biology 3 (2001) 1086–1091.
date_created: 2022-04-07T07:57:42Z
date_published: 2001-11-02T00:00:00Z
date_updated: 2022-07-18T08:58:07Z
day: '02'
doi: 10.1038/ncb1201-1086
extern: '1'
external_id:
pmid:
- '11781570'
intvolume: ' 3'
issue: '12'
keyword:
- Cell Biology
language:
- iso: eng
month: '11'
oa_version: None
page: 1086-1091
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: Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 3
year: '2001'
...
---
_id: '11126'
abstract:
- lang: eng
text: Nuclear import of the two uracil-rich small nuclear ribonucleoprotein (U snRNP)
components U1A and U2B′′ is mediated by unusually long and complex nuclear localization
signals (NLSs). Here we investigate nuclear import of U1A and U2B′′ in vitro and
demonstrate that it occurs by an active, saturable process. Several lines of evidence
suggest that import of the two proteins occurs by an import mechanism different
to those characterized previously. No cross competition is seen with a variety
of previously studied NLSs. In contrast to import mediated by members of the importin-β
family of nucleocytoplasmic transport receptors, U1A/U2B′′ import is not inhibited
by either nonhydrolyzable guanosine triphosphate (GTP) analogues or by a mutant
of the GTPase Ran that is incapable of GTP hydrolysis. Adenosine triphosphate
is capable of supporting U1A and U2B′′ import, whereas neither nonhydrolyzable
adenosine triphosphate analogues nor GTP can do so. U1A and U2B′′ import in vitro
does not require the addition of soluble cytosolic proteins, but a factor or factors
required for U1A and U2B′′ import remains tightly associated with the nuclear
fraction of conventionally permeabilized cells. This activity can be solubilized
in the presence of elevated MgCl2. These data suggest that U1A and U2B′′ import
into the nucleus occurs by a hitherto uncharacterized mechanism.
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
- first_name: Iain W.
full_name: Mattaj, Iain W.
last_name: Mattaj
citation:
ama: Hetzer M, Mattaj IW. An Atp-dependent, Ran-independent mechanism for nuclear
import of the U1a and U2b′′ spliceosome proteins. Journal of Cell Biology.
2000;148(2):293-304. doi:10.1083/jcb.148.2.293
apa: Hetzer, M., & Mattaj, I. W. (2000). An Atp-dependent, Ran-independent mechanism
for nuclear import of the U1a and U2b′′ spliceosome proteins. Journal of Cell
Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.148.2.293
chicago: Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent
Mechanism for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” Journal
of Cell Biology. Rockefeller University Press, 2000. https://doi.org/10.1083/jcb.148.2.293.
ieee: M. Hetzer and I. W. Mattaj, “An Atp-dependent, Ran-independent mechanism for
nuclear import of the U1a and U2b′′ spliceosome proteins,” Journal of Cell
Biology, vol. 148, no. 2. Rockefeller University Press, pp. 293–304, 2000.
ista: Hetzer M, Mattaj IW. 2000. An Atp-dependent, Ran-independent mechanism for
nuclear import of the U1a and U2b′′ spliceosome proteins. Journal of Cell Biology.
148(2), 293–304.
mla: Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent Mechanism
for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” Journal of Cell
Biology, vol. 148, no. 2, Rockefeller University Press, 2000, pp. 293–304,
doi:10.1083/jcb.148.2.293.
short: M. Hetzer, I.W. Mattaj, Journal of Cell Biology 148 (2000) 293–304.
date_created: 2022-04-07T07:57:49Z
date_published: 2000-01-24T00:00:00Z
date_updated: 2022-07-18T08:58:29Z
day: '24'
doi: 10.1083/jcb.148.2.293
extern: '1'
external_id:
pmid:
- '10648562'
intvolume: ' 148'
issue: '2'
keyword:
- Cell Biology
language:
- iso: eng
month: '01'
oa_version: None
page: 293-304
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: An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and
U2b′′ spliceosome proteins
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 148
year: '2000'
...
---
_id: '11127'
abstract:
- lang: eng
text: Nuclear formation in Xenopus egg extracts requires cytosol and is inhibited
by GTPγS, indicating a requirement for GTPase activity. Nuclear envelope (NE)
vesicle fusion is extensively inhibited by GTPγS and two mutant forms of the Ran
GTPase, Q69L and T24N. Depletion of either Ran or RCC1, the exchange factor for
Ran, from the assembly reaction also inhibits this step of NE formation. Ran depletion
can be complemented by the addition of Ran loaded with either GTP or GDP but not
with GTPγS. RCC1 depletion is only complemented by RCC1 itself or by RanGTP. Thus,
generation of RanGTP by RCC1 and GTP hydrolysis by Ran are both required for the
extensive membrane fusion events that lead to NE formation.
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
- first_name: Daniel
full_name: Bilbao-Cortés, Daniel
last_name: Bilbao-Cortés
- first_name: Tobias C
full_name: Walther, Tobias C
last_name: Walther
- first_name: Oliver J
full_name: Gruss, Oliver J
last_name: Gruss
- first_name: Iain W
full_name: Mattaj, Iain W
last_name: Mattaj
citation:
ama: Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. GTP hydrolysis
by Ran is required for nuclear envelope assembly. Molecular Cell. 2000;5(6):1013-1024.
doi:10.1016/s1097-2765(00)80266-x
apa: Hetzer, M., Bilbao-Cortés, D., Walther, T. C., Gruss, O. J., & Mattaj,
I. W. (2000). GTP hydrolysis by Ran is required for nuclear envelope assembly.
Molecular Cell. Elsevier. https://doi.org/10.1016/s1097-2765(00)80266-x
chicago: Hetzer, Martin, Daniel Bilbao-Cortés, Tobias C Walther, Oliver J Gruss,
and Iain W Mattaj. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.”
Molecular Cell. Elsevier, 2000. https://doi.org/10.1016/s1097-2765(00)80266-x.
ieee: M. Hetzer, D. Bilbao-Cortés, T. C. Walther, O. J. Gruss, and I. W. Mattaj,
“GTP hydrolysis by Ran is required for nuclear envelope assembly,” Molecular
Cell, vol. 5, no. 6. Elsevier, pp. 1013–1024, 2000.
ista: Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. 2000. GTP hydrolysis
by Ran is required for nuclear envelope assembly. Molecular Cell. 5(6), 1013–1024.
mla: Hetzer, Martin, et al. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope
Assembly.” Molecular Cell, vol. 5, no. 6, Elsevier, 2000, pp. 1013–24,
doi:10.1016/s1097-2765(00)80266-x.
short: M. Hetzer, D. Bilbao-Cortés, T.C. Walther, O.J. Gruss, I.W. Mattaj, Molecular
Cell 5 (2000) 1013–1024.
date_created: 2022-04-07T07:57:59Z
date_published: 2000-06-01T00:00:00Z
date_updated: 2022-07-18T08:58:31Z
day: '01'
doi: 10.1016/s1097-2765(00)80266-x
extern: '1'
external_id:
pmid:
- '10911995'
intvolume: ' 5'
issue: '6'
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language:
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url: https://doi.org/10.1016/S1097-2765(00)80266-X
month: '06'
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oa_version: Published Version
page: 1013-1024
pmid: 1
publication: Molecular Cell
publication_identifier:
issn:
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publication_status: published
publisher: Elsevier
quality_controlled: '1'
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status: public
title: GTP hydrolysis by Ran is required for nuclear envelope assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 5
year: '2000'
...