---
_id: '9629'
abstract:
- lang: eng
  text: Intestinal organoids derived from single cells undergo complex crypt–villus
    patterning and morphogenesis. However, the nature and coordination of the underlying
    forces remains poorly characterized. Here, using light-sheet microscopy and large-scale
    imaging quantification, we demonstrate that crypt formation coincides with a stark
    reduction in lumen volume. We develop a 3D biophysical model to computationally
    screen different mechanical scenarios of crypt morphogenesis. Combining this with
    live-imaging data and multiple mechanical perturbations, we show that actomyosin-driven
    crypt apical contraction and villus basal tension work synergistically with lumen
    volume reduction to drive crypt morphogenesis, and demonstrate the existence of
    a critical point in differential tensions above which crypt morphology becomes
    robust to volume changes. Finally, we identified a sodium/glucose cotransporter
    that is specific to differentiated enterocytes that modulates lumen volume reduction
    through cell swelling in the villus region. Together, our study uncovers the cellular
    basis of how cell fate modulates osmotic and actomyosin forces to coordinate robust
    morphogenesis.
acknowledgement: 'We acknowledge the members of the Lennon-Duménil laboratory for
  sharing the mouse line of Myh9-GFP. We are grateful to the members of the Liberali
  laboratory and the FMI facilities for their support. We thank E. Tagliavini for
  IT support; L. Gelman for assistance and training; S. Bichet and A. Bogucki for
  helping with histology of mouse tissues; H. Kohler for fluorescence-activated cell
  sorting; G. Q. G. de Medeiros for maintenance of light-sheet microscopy; M. G. Stadler
  for scRNA-seq analysis; G. Gay for discussions on the 3D vertex model; the members
  of the Liberali laboratory, C. P. Heisenberg and C. Tsiairis for reading and providing
  feedback on the manuscript. Funding: Q.Y. is supported by a Postdoc fellowship from
  Peter und Taul Engelhorn Stiftung (PTES). This work received funding from the European
  Research Council (ERC) under the EU Horizon 2020 research and Innovation Programme
  Grant Agreement no. 758617 (to P.L.), the Swiss National Foundation (SNF) (POOP3_157531,
  to P.L.) and from the ERC under the EU Horizon 2020 Research and Innovation Program
  Grant Agreements 851288 (to E.H.) and the Austrian Science Fund (FWF) (P31639, to
  E.H.).'
article_processing_charge: No
article_type: original
author:
- first_name: Qiutan
  full_name: Yang, Qiutan
  last_name: Yang
- first_name: Shi-lei
  full_name: Xue, Shi-lei
  id: 31D2C804-F248-11E8-B48F-1D18A9856A87
  last_name: Xue
- first_name: Chii Jou
  full_name: Chan, Chii Jou
  last_name: Chan
- first_name: Markus
  full_name: Rempfler, Markus
  last_name: Rempfler
- first_name: Dario
  full_name: Vischi, Dario
  last_name: Vischi
- first_name: Francisca
  full_name: Maurer-Gutierrez, Francisca
  last_name: Maurer-Gutierrez
- first_name: Takashi
  full_name: Hiiragi, Takashi
  last_name: Hiiragi
- first_name: Edouard B
  full_name: Hannezo, Edouard B
  id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
  last_name: Hannezo
  orcid: 0000-0001-6005-1561
- first_name: Prisca
  full_name: Liberali, Prisca
  last_name: Liberali
citation:
  ama: Yang Q, Xue S, Chan CJ, et al. Cell fate coordinates mechano-osmotic forces
    in intestinal crypt formation. <i>Nature Cell Biology</i>. 2021;23:733–744. doi:<a
    href="https://doi.org/10.1038/s41556-021-00700-2">10.1038/s41556-021-00700-2</a>
  apa: Yang, Q., Xue, S., Chan, C. J., Rempfler, M., Vischi, D., Maurer-Gutierrez,
    F., … Liberali, P. (2021). Cell fate coordinates mechano-osmotic forces in intestinal
    crypt formation. <i>Nature Cell Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41556-021-00700-2">https://doi.org/10.1038/s41556-021-00700-2</a>
  chicago: Yang, Qiutan, Shi-lei Xue, Chii Jou Chan, Markus Rempfler, Dario Vischi,
    Francisca Maurer-Gutierrez, Takashi Hiiragi, Edouard B Hannezo, and Prisca Liberali.
    “Cell Fate Coordinates Mechano-Osmotic Forces in Intestinal Crypt Formation.”
    <i>Nature Cell Biology</i>. Springer Nature, 2021. <a href="https://doi.org/10.1038/s41556-021-00700-2">https://doi.org/10.1038/s41556-021-00700-2</a>.
  ieee: Q. Yang <i>et al.</i>, “Cell fate coordinates mechano-osmotic forces in intestinal
    crypt formation,” <i>Nature Cell Biology</i>, vol. 23. Springer Nature, pp. 733–744,
    2021.
  ista: Yang Q, Xue S, Chan CJ, Rempfler M, Vischi D, Maurer-Gutierrez F, Hiiragi
    T, Hannezo EB, Liberali P. 2021. Cell fate coordinates mechano-osmotic forces
    in intestinal crypt formation. Nature Cell Biology. 23, 733–744.
  mla: Yang, Qiutan, et al. “Cell Fate Coordinates Mechano-Osmotic Forces in Intestinal
    Crypt Formation.” <i>Nature Cell Biology</i>, vol. 23, Springer Nature, 2021,
    pp. 733–744, doi:<a href="https://doi.org/10.1038/s41556-021-00700-2">10.1038/s41556-021-00700-2</a>.
  short: Q. Yang, S. Xue, C.J. Chan, M. Rempfler, D. Vischi, F. Maurer-Gutierrez,
    T. Hiiragi, E.B. Hannezo, P. Liberali, Nature Cell Biology 23 (2021) 733–744.
date_created: 2021-07-04T22:01:25Z
date_published: 2021-06-21T00:00:00Z
date_updated: 2023-08-10T13:57:36Z
day: '21'
department:
- _id: EdHa
doi: 10.1038/s41556-021-00700-2
ec_funded: 1
external_id:
  isi:
  - '000664016300003'
  pmid:
  - '34155381'
intvolume: '        23'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://www.biorxiv.org/content/10.1101/2020.05.13.094359
month: '06'
oa: 1
oa_version: Preprint
page: 733–744
pmid: 1
project:
- _id: 05943252-7A3F-11EA-A408-12923DDC885E
  call_identifier: H2020
  grant_number: '851288'
  name: Design Principles of Branching Morphogenesis
- _id: 268294B6-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: P31639
  name: Active mechano-chemical description of the cell cytoskeleton
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: Cell fate coordinates mechano-osmotic forces in intestinal crypt formation
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 23
year: '2021'
...
---
_id: '6837'
abstract:
- lang: eng
  text: Migrasomes are a recently discovered type of extracellular vesicles that are
    characteristically generated along retraction fibers in migrating cells. Two studies
    now show how migrasomes are formed and how they function in the physiologically
    relevant context of the developing zebrafish embryo.
article_processing_charge: No
author:
- first_name: Ste
  full_name: Tavano, Ste
  id: 2F162F0C-F248-11E8-B48F-1D18A9856A87
  last_name: Tavano
  orcid: 0000-0001-9970-7804
- first_name: Carl-Philipp J
  full_name: Heisenberg, Carl-Philipp J
  id: 39427864-F248-11E8-B48F-1D18A9856A87
  last_name: Heisenberg
  orcid: 0000-0002-0912-4566
citation:
  ama: Tavano S, Heisenberg C-PJ. Migrasomes take center stage. <i>Nature Cell Biology</i>.
    2019;21(8):918-920. doi:<a href="https://doi.org/10.1038/s41556-019-0369-3">10.1038/s41556-019-0369-3</a>
  apa: Tavano, S., &#38; Heisenberg, C.-P. J. (2019). Migrasomes take center stage.
    <i>Nature Cell Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41556-019-0369-3">https://doi.org/10.1038/s41556-019-0369-3</a>
  chicago: Tavano, Ste, and Carl-Philipp J Heisenberg. “Migrasomes Take Center Stage.”
    <i>Nature Cell Biology</i>. Springer Nature, 2019. <a href="https://doi.org/10.1038/s41556-019-0369-3">https://doi.org/10.1038/s41556-019-0369-3</a>.
  ieee: S. Tavano and C.-P. J. Heisenberg, “Migrasomes take center stage,” <i>Nature
    Cell Biology</i>, vol. 21, no. 8. Springer Nature, pp. 918–920, 2019.
  ista: Tavano S, Heisenberg C-PJ. 2019. Migrasomes take center stage. Nature Cell
    Biology. 21(8), 918–920.
  mla: Tavano, Ste, and Carl-Philipp J. Heisenberg. “Migrasomes Take Center Stage.”
    <i>Nature Cell Biology</i>, vol. 21, no. 8, Springer Nature, 2019, pp. 918–20,
    doi:<a href="https://doi.org/10.1038/s41556-019-0369-3">10.1038/s41556-019-0369-3</a>.
  short: S. Tavano, C.-P.J. Heisenberg, Nature Cell Biology 21 (2019) 918–920.
date_created: 2019-09-01T22:00:57Z
date_published: 2019-08-01T00:00:00Z
date_updated: 2023-08-29T07:42:20Z
day: '01'
department:
- _id: CaHe
doi: 10.1038/s41556-019-0369-3
external_id:
  isi:
  - '000478029000003'
  pmid:
  - '31371826'
intvolume: '        21'
isi: 1
issue: '8'
language:
- iso: eng
month: '08'
oa_version: None
page: 918-920
pmid: 1
publication: Nature Cell Biology
publication_identifier:
  eissn:
  - 1476-4679
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Migrasomes take center stage
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 21
year: '2019'
...
---
_id: '7105'
abstract:
- lang: eng
  text: Cell migration is hypothesized to involve a cycle of behaviours beginning
    with leading edge extension. However, recent evidence suggests that the leading
    edge may be dispensable for migration, raising the question of what actually controls
    cell directionality. Here, we exploit the embryonic migration of Drosophila macrophages
    to bridge the different temporal scales of the behaviours controlling motility.
    This approach reveals that edge fluctuations during random motility are not persistent
    and are weakly correlated with motion. In contrast, flow of the actin network
    behind the leading edge is highly persistent. Quantification of actin flow structure
    during migration reveals a stable organization and asymmetry in the cell-wide
    flowfield that strongly correlates with cell directionality. This organization
    is regulated by a gradient of actin network compression and destruction, which
    is controlled by myosin contraction and cofilin-mediated disassembly. It is this
    stable actin-flow polarity, which integrates rapid fluctuations of the leading
    edge, that controls inherent cellular persistence.
article_processing_charge: No
article_type: original
author:
- first_name: Lawrence
  full_name: Yolland, Lawrence
  last_name: Yolland
- first_name: Mubarik
  full_name: Burki, Mubarik
  last_name: Burki
- first_name: Stefania
  full_name: Marcotti, Stefania
  last_name: Marcotti
- first_name: Andrei
  full_name: Luchici, Andrei
  last_name: Luchici
- first_name: Fiona N.
  full_name: Kenny, Fiona N.
  last_name: Kenny
- first_name: John Robert
  full_name: Davis, John Robert
  last_name: Davis
- first_name: Eduardo
  full_name: Serna-Morales, Eduardo
  last_name: Serna-Morales
- first_name: Jan
  full_name: Müller, Jan
  id: AD07FDB4-0F61-11EA-8158-C4CC64CEAA8D
  last_name: Müller
- first_name: Michael K
  full_name: Sixt, Michael K
  id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
  last_name: Sixt
  orcid: 0000-0002-6620-9179
- first_name: Andrew
  full_name: Davidson, Andrew
  last_name: Davidson
- first_name: Will
  full_name: Wood, Will
  last_name: Wood
- first_name: Linus J.
  full_name: Schumacher, Linus J.
  last_name: Schumacher
- first_name: Robert G.
  full_name: Endres, Robert G.
  last_name: Endres
- first_name: Mark
  full_name: Miodownik, Mark
  last_name: Miodownik
- first_name: Brian M.
  full_name: Stramer, Brian M.
  last_name: Stramer
citation:
  ama: Yolland L, Burki M, Marcotti S, et al. Persistent and polarized global actin
    flow is essential for directionality during cell migration. <i>Nature Cell Biology</i>.
    2019;21(11):1370-1381. doi:<a href="https://doi.org/10.1038/s41556-019-0411-5">10.1038/s41556-019-0411-5</a>
  apa: Yolland, L., Burki, M., Marcotti, S., Luchici, A., Kenny, F. N., Davis, J.
    R., … Stramer, B. M. (2019). Persistent and polarized global actin flow is essential
    for directionality during cell migration. <i>Nature Cell Biology</i>. Springer
    Nature. <a href="https://doi.org/10.1038/s41556-019-0411-5">https://doi.org/10.1038/s41556-019-0411-5</a>
  chicago: Yolland, Lawrence, Mubarik Burki, Stefania Marcotti, Andrei Luchici, Fiona
    N. Kenny, John Robert Davis, Eduardo Serna-Morales, et al. “Persistent and Polarized
    Global Actin Flow Is Essential for Directionality during Cell Migration.” <i>Nature
    Cell Biology</i>. Springer Nature, 2019. <a href="https://doi.org/10.1038/s41556-019-0411-5">https://doi.org/10.1038/s41556-019-0411-5</a>.
  ieee: L. Yolland <i>et al.</i>, “Persistent and polarized global actin flow is essential
    for directionality during cell migration,” <i>Nature Cell Biology</i>, vol. 21,
    no. 11. Springer Nature, pp. 1370–1381, 2019.
  ista: Yolland L, Burki M, Marcotti S, Luchici A, Kenny FN, Davis JR, Serna-Morales
    E, Müller J, Sixt MK, Davidson A, Wood W, Schumacher LJ, Endres RG, Miodownik
    M, Stramer BM. 2019. Persistent and polarized global actin flow is essential for
    directionality during cell migration. Nature Cell Biology. 21(11), 1370–1381.
  mla: Yolland, Lawrence, et al. “Persistent and Polarized Global Actin Flow Is Essential
    for Directionality during Cell Migration.” <i>Nature Cell Biology</i>, vol. 21,
    no. 11, Springer Nature, 2019, pp. 1370–81, doi:<a href="https://doi.org/10.1038/s41556-019-0411-5">10.1038/s41556-019-0411-5</a>.
  short: L. Yolland, M. Burki, S. Marcotti, A. Luchici, F.N. Kenny, J.R. Davis, E.
    Serna-Morales, J. Müller, M.K. Sixt, A. Davidson, W. Wood, L.J. Schumacher, R.G.
    Endres, M. Miodownik, B.M. Stramer, Nature Cell Biology 21 (2019) 1370–1381.
date_created: 2019-11-25T08:55:00Z
date_published: 2019-11-01T00:00:00Z
date_updated: 2023-09-06T11:08:52Z
day: '01'
department:
- _id: MiSi
doi: 10.1038/s41556-019-0411-5
external_id:
  isi:
  - '000495888300009'
  pmid:
  - '31685997'
intvolume: '        21'
isi: 1
issue: '11'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7025891
month: '11'
oa: 1
oa_version: Submitted Version
page: 1370-1381
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: Persistent and polarized global actin flow is essential for directionality
  during cell migration
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 21
year: '2019'
...
---
_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. <i>Nature Cell Biology</i>. 2007;9(10):1160-1166.
    doi:<a href="https://doi.org/10.1038/ncb1636">10.1038/ncb1636</a>
  apa: Anderson, D. J., &#38; Hetzer, M. (2007). Nuclear envelope formation by chromatin-mediated
    reorganization of the endoplasmic reticulum. <i>Nature Cell Biology</i>. Springer
    Nature. <a href="https://doi.org/10.1038/ncb1636">https://doi.org/10.1038/ncb1636</a>
  chicago: Anderson, Daniel J., and Martin Hetzer. “Nuclear Envelope Formation by
    Chromatin-Mediated Reorganization of the Endoplasmic Reticulum.” <i>Nature Cell
    Biology</i>. Springer Nature, 2007. <a href="https://doi.org/10.1038/ncb1636">https://doi.org/10.1038/ncb1636</a>.
  ieee: D. J. Anderson and M. Hetzer, “Nuclear envelope formation by chromatin-mediated
    reorganization of the endoplasmic reticulum,” <i>Nature Cell Biology</i>, 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.” <i>Nature Cell Biology</i>, vol.
    9, no. 10, Springer Nature, 2007, pp. 1160–66, doi:<a href="https://doi.org/10.1038/ncb1636">10.1038/ncb1636</a>.
  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: '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. <i>Nature Cell Biology</i>.
    2002;4(7):E177-E184. doi:<a href="https://doi.org/10.1038/ncb0702-e177">10.1038/ncb0702-e177</a>
  apa: Hetzer, M., Gruss, O. J., &#38; Mattaj, I. W. (2002). The Ran GTPase as a marker
    of chromosome position in spindle formation and nuclear envelope assembly. <i>Nature
    Cell Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/ncb0702-e177">https://doi.org/10.1038/ncb0702-e177</a>
  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.”
    <i>Nature Cell Biology</i>. Springer Nature, 2002. <a href="https://doi.org/10.1038/ncb0702-e177">https://doi.org/10.1038/ncb0702-e177</a>.
  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,” <i>Nature Cell Biology</i>,
    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.” <i>Nature Cell Biology</i>,
    vol. 4, no. 7, Springer Nature, 2002, pp. E177–84, doi:<a href="https://doi.org/10.1038/ncb0702-e177">10.1038/ncb0702-e177</a>.
  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: '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. <i>Nature
    Cell Biology</i>. 2001;3(12):1086-1091. doi:<a href="https://doi.org/10.1038/ncb1201-1086">10.1038/ncb1201-1086</a>
  apa: Hetzer, M., Meyer, H. H., Walther, T. C., Bilbao-Cortes, D., Warren, G., &#38;
    Mattaj, I. W. (2001). Distinct AAA-ATPase p97 complexes function in discrete steps
    of nuclear assembly. <i>Nature Cell Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/ncb1201-1086">https://doi.org/10.1038/ncb1201-1086</a>
  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.” <i>Nature Cell Biology</i>. Springer Nature,
    2001. <a href="https://doi.org/10.1038/ncb1201-1086">https://doi.org/10.1038/ncb1201-1086</a>.
  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,” <i>Nature Cell Biology</i>, 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.” <i>Nature Cell Biology</i>, vol. 3, no. 12, Springer
    Nature, 2001, pp. 1086–91, doi:<a href="https://doi.org/10.1038/ncb1201-1086">10.1038/ncb1201-1086</a>.
  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'
...