---
_id: '11081'
abstract:
- lang: eng
text: In eukaryotic cells the nuclear genome is enclosed by the nuclear envelope
(NE). In metazoans, the NE breaks down in mitosis and it has been assumed that
the physical barrier separating nucleoplasm and cytoplasm remains intact during
the rest of the cell cycle and cell differentiation. However, recent studies suggest
that nonmitotic NE remodeling plays a critical role in development, virus infection,
laminopathies, and cancer. Although the mechanisms underlying these NE restructuring
events are currently being defined, one common theme is activation of protein
kinase C family members in the interphase nucleus to disrupt the nuclear lamina,
demonstrating the importance of the lamina in maintaining nuclear integrity.
article_processing_charge: No
article_type: review
author:
- first_name: Emily
full_name: Hatch, Emily
last_name: Hatch
- 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: Hatch E, Hetzer M. Breaching the nuclear envelope in development and disease.
Journal of Cell Biology. 2014;205(2):133-141. doi:10.1083/jcb.201402003
apa: Hatch, E., & Hetzer, M. (2014). Breaching the nuclear envelope in development
and disease. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.201402003
chicago: Hatch, Emily, and Martin Hetzer. “Breaching the Nuclear Envelope in Development
and Disease.” Journal of Cell Biology. Rockefeller University Press, 2014.
https://doi.org/10.1083/jcb.201402003.
ieee: E. Hatch and M. Hetzer, “Breaching the nuclear envelope in development and
disease,” Journal of Cell Biology, vol. 205, no. 2. Rockefeller University
Press, pp. 133–141, 2014.
ista: Hatch E, Hetzer M. 2014. Breaching the nuclear envelope in development and
disease. Journal of Cell Biology. 205(2), 133–141.
mla: Hatch, Emily, and Martin Hetzer. “Breaching the Nuclear Envelope in Development
and Disease.” Journal of Cell Biology, vol. 205, no. 2, Rockefeller University
Press, 2014, pp. 133–41, doi:10.1083/jcb.201402003.
short: E. Hatch, M. Hetzer, Journal of Cell Biology 205 (2014) 133–141.
date_created: 2022-04-07T07:50:13Z
date_published: 2014-04-21T00:00:00Z
date_updated: 2024-10-14T11:23:23Z
day: '21'
doi: 10.1083/jcb.201402003
extern: '1'
external_id:
pmid:
- '24751535'
intvolume: ' 205'
issue: '2'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.201402003
month: '04'
oa: 1
oa_version: Published Version
page: 133-141
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
issn:
- 1540-8140
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Breaching the nuclear envelope in development and disease
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 205
year: '2014'
...
---
_id: '11082'
abstract:
- lang: eng
text: The nuclear pore complex (NPC) plays a critical role in gene expression by
mediating import of transcription regulators into the nucleus and export of RNA
transcripts to the cytoplasm. Emerging evidence suggests that in addition to mediating
transport, a subset of nucleoporins (Nups) engage in transcriptional activation
and elongation at genomic loci that are not associated with NPCs. The underlying
mechanism and regulation of Nup mobility on and off nuclear pores remain unclear.
Here we show that Nup50 is a mobile Nup with a pronounced presence both at the
NPC and in the nucleoplasm that can move between these different localizations.
Strikingly, the dynamic behavior of Nup50 in both locations is dependent on active
transcription by RNA polymerase II and requires the N-terminal half of the protein,
which contains importin α– and Nup153-binding domains. However, Nup50 dynamics
are independent of importin α, Nup153, and Nup98, even though the latter two proteins
also exhibit transcription-dependent mobility. Of interest, depletion of Nup50
from C2C12 myoblasts does not affect cell proliferation but inhibits differentiation
into myotubes. Taken together, our results suggest a transport-independent role
for Nup50 in chromatin biology that occurs away from the NPC.
article_processing_charge: No
article_type: original
author:
- first_name: Abigail L.
full_name: Buchwalter, Abigail L.
last_name: Buchwalter
- first_name: Yun
full_name: Liang, Yun
last_name: Liang
- 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: Buchwalter AL, Liang Y, Hetzer M. Nup50 is required for cell differentiation
and exhibits transcription-dependent dynamics. Molecular Biology of the Cell.
2014;25(16):2472-2484. doi:10.1091/mbc.e14-04-0865
apa: Buchwalter, A. L., Liang, Y., & Hetzer, M. (2014). Nup50 is required for
cell differentiation and exhibits transcription-dependent dynamics. Molecular
Biology of the Cell. American Society for Cell Biology. https://doi.org/10.1091/mbc.e14-04-0865
chicago: Buchwalter, Abigail L., Yun Liang, and Martin Hetzer. “Nup50 Is Required
for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” Molecular
Biology of the Cell. American Society for Cell Biology, 2014. https://doi.org/10.1091/mbc.e14-04-0865.
ieee: A. L. Buchwalter, Y. Liang, and M. Hetzer, “Nup50 is required for cell differentiation
and exhibits transcription-dependent dynamics,” Molecular Biology of the Cell,
vol. 25, no. 16. American Society for Cell Biology, pp. 2472–2484, 2014.
ista: Buchwalter AL, Liang Y, Hetzer M. 2014. Nup50 is required for cell differentiation
and exhibits transcription-dependent dynamics. Molecular Biology of the Cell.
25(16), 2472–2484.
mla: Buchwalter, Abigail L., et al. “Nup50 Is Required for Cell Differentiation
and Exhibits Transcription-Dependent Dynamics.” Molecular Biology of the Cell,
vol. 25, no. 16, American Society for Cell Biology, 2014, pp. 2472–84, doi:10.1091/mbc.e14-04-0865.
short: A.L. Buchwalter, Y. Liang, M. Hetzer, Molecular Biology of the Cell 25 (2014)
2472–2484.
date_created: 2022-04-07T07:50:24Z
date_published: 2014-08-15T00:00:00Z
date_updated: 2024-10-14T11:23:34Z
day: '15'
doi: 10.1091/mbc.e14-04-0865
extern: '1'
intvolume: ' 25'
issue: '16'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1091/mbc.e14-04-0865
month: '08'
oa: 1
oa_version: Published Version
page: 2472-2484
publication: Molecular Biology of the Cell
publication_identifier:
issn:
- 1059-1524
- 1939-4586
publication_status: published
publisher: American Society for Cell Biology
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nup50 is required for cell differentiation and exhibits transcription-dependent
dynamics
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 25
year: '2014'
...
---
_id: '11083'
abstract:
- lang: eng
text: Nuclear pore complex (NPC) proteins are known for their critical roles in
regulating nucleocytoplasmic traffic of macromolecules across the nuclear envelope.
However, recent findings suggest that some nucleoporins (Nups), including Nup98,
have additional functions in developmental gene regulation. Nup98, which exhibits
transcription-dependent mobility at the NPC but can also bind chromatin away from
the nuclear envelope, is frequently involved in chromosomal translocations in
a subset of patients suffering from acute myeloid leukemia (AML). A common paradigm
suggests that Nup98 translocations cause aberrant transcription when they are
recuited to aberrant genomic loci. Importantly, this model fails to account for
the potential loss of wild type (WT) Nup98 function in the presence of Nup98 translocation
mutants. Here we examine how the cell might regulate Nup98 nucleoplasmic protein
levels to control transcription in healthy cells. In addition, we discuss the
possibility that dominant negative Nup98 fusion proteins disrupt the transcriptional
activity of WT Nup98 in the nucleoplasm to drive AML.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Tobias M.
full_name: Franks, Tobias M.
last_name: Franks
- 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: Franks TM, Hetzer M. The role of Nup98 in transcription regulation in healthy
and diseased cells. Trends in Cell Biology. 2013;23(3):112-117. doi:10.1016/j.tcb.2012.10.013
apa: Franks, T. M., & Hetzer, M. (2013). The role of Nup98 in transcription
regulation in healthy and diseased cells. Trends in Cell Biology. Elsevier.
https://doi.org/10.1016/j.tcb.2012.10.013
chicago: Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription
Regulation in Healthy and Diseased Cells.” Trends in Cell Biology. Elsevier,
2013. https://doi.org/10.1016/j.tcb.2012.10.013.
ieee: T. M. Franks and M. Hetzer, “The role of Nup98 in transcription regulation
in healthy and diseased cells,” Trends in Cell Biology, vol. 23, no. 3.
Elsevier, pp. 112–117, 2013.
ista: Franks TM, Hetzer M. 2013. The role of Nup98 in transcription regulation in
healthy and diseased cells. Trends in Cell Biology. 23(3), 112–117.
mla: Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation
in Healthy and Diseased Cells.” Trends in Cell Biology, vol. 23, no. 3,
Elsevier, 2013, pp. 112–17, doi:10.1016/j.tcb.2012.10.013.
short: T.M. Franks, M. Hetzer, Trends in Cell Biology 23 (2013) 112–117.
date_created: 2022-04-07T07:50:33Z
date_published: 2013-03-01T00:00:00Z
date_updated: 2024-10-14T11:23:44Z
day: '01'
doi: 10.1016/j.tcb.2012.10.013
extern: '1'
external_id:
pmid:
- '23246429'
intvolume: ' 23'
issue: '3'
keyword:
- Cell Biology
language:
- iso: eng
month: '03'
oa_version: None
page: 112-117
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: The role of Nup98 in transcription regulation in healthy and diseased cells
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2013'
...
---
_id: '11084'
abstract:
- lang: eng
text: Protein turnover is an effective way of maintaining a functional proteome,
as old and potentially damaged polypeptides are destroyed and replaced by newly
synthesized copies. An increasing number of intracellular proteins, however, have
been identified that evade this turnover process and instead are maintained over
a cell's lifetime. This diverse group of long-lived proteins might be particularly
prone to accumulation of damage and thus have a crucial role in the functional
deterioration of key regulatory processes during ageing.
article_processing_charge: No
article_type: original
author:
- first_name: Brandon H.
full_name: Toyama, Brandon H.
last_name: Toyama
- 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: 'Toyama BH, Hetzer M. Protein homeostasis: Live long, won’t prosper. Nature
Reviews Molecular Cell Biology. 2013;14:55-61. doi:10.1038/nrm3496'
apa: 'Toyama, B. H., & Hetzer, M. (2013). Protein homeostasis: Live long, won’t
prosper. Nature Reviews Molecular Cell Biology. Springer Nature. https://doi.org/10.1038/nrm3496'
chicago: 'Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long,
Won’t Prosper.” Nature Reviews Molecular Cell Biology. Springer Nature,
2013. https://doi.org/10.1038/nrm3496.'
ieee: 'B. H. Toyama and M. Hetzer, “Protein homeostasis: Live long, won’t prosper,”
Nature Reviews Molecular Cell Biology, vol. 14. Springer Nature, pp. 55–61,
2013.'
ista: 'Toyama BH, Hetzer M. 2013. Protein homeostasis: Live long, won’t prosper.
Nature Reviews Molecular Cell Biology. 14, 55–61.'
mla: 'Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t
Prosper.” Nature Reviews Molecular Cell Biology, vol. 14, Springer Nature,
2013, pp. 55–61, doi:10.1038/nrm3496.'
short: B.H. Toyama, M. Hetzer, Nature Reviews Molecular Cell Biology 14 (2013) 55–61.
date_created: 2022-04-07T07:50:43Z
date_published: 2013-01-01T00:00:00Z
date_updated: 2024-10-14T11:24:09Z
day: '01'
doi: 10.1038/nrm3496
extern: '1'
external_id:
pmid:
- '23258296'
intvolume: ' 14'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
month: '01'
oa_version: None
page: 55-61
pmid: 1
publication: Nature Reviews Molecular Cell Biology
publication_identifier:
issn:
- 1471-0072
- 1471-0080
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Protein homeostasis: Live long, won''t prosper'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 14
year: '2013'
...
---
_id: '11089'
abstract:
- lang: eng
text: The Nuclear Envelope (NE) contains over 100 different proteins that associate
with nuclear components such as chromatin, the lamina and the transcription machinery.
Mutations in genes encoding NE proteins have been shown to result in tissue-specific
defects and disease, suggesting cell-type specific differences in NE composition
and function. Consistent with these observations, recent studies have revealed
unexpected functions for numerous NE associated proteins during cell differentiation
and development. Here we review the latest insights into the roles played by the
NE in cell differentiation, development, disease and aging, focusing primarily
on inner nuclear membrane (INM) proteins and nuclear pore components.
article_processing_charge: No
article_type: original
author:
- first_name: J Sebastian
full_name: Gomez-Cavazos, J Sebastian
last_name: Gomez-Cavazos
- 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: 'Gomez-Cavazos JS, Hetzer M. Outfits for different occasions: tissue-specific
roles of Nuclear Envelope proteins. Current Opinion in Cell Biology. 2012;24(6):775-783.
doi:10.1016/j.ceb.2012.08.008'
apa: 'Gomez-Cavazos, J. S., & Hetzer, M. (2012). Outfits for different occasions:
tissue-specific roles of Nuclear Envelope proteins. Current Opinion in Cell
Biology. Elsevier. https://doi.org/10.1016/j.ceb.2012.08.008'
chicago: 'Gomez-Cavazos, J Sebastian, and Martin Hetzer. “Outfits for Different
Occasions: Tissue-Specific Roles of Nuclear Envelope Proteins.” Current Opinion
in Cell Biology. Elsevier, 2012. https://doi.org/10.1016/j.ceb.2012.08.008.'
ieee: 'J. S. Gomez-Cavazos and M. Hetzer, “Outfits for different occasions: tissue-specific
roles of Nuclear Envelope proteins,” Current Opinion in Cell Biology, vol.
24, no. 6. Elsevier, pp. 775–783, 2012.'
ista: 'Gomez-Cavazos JS, Hetzer M. 2012. Outfits for different occasions: tissue-specific
roles of Nuclear Envelope proteins. Current Opinion in Cell Biology. 24(6), 775–783.'
mla: 'Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “Outfits for Different Occasions:
Tissue-Specific Roles of Nuclear Envelope Proteins.” Current Opinion in Cell
Biology, vol. 24, no. 6, Elsevier, 2012, pp. 775–83, doi:10.1016/j.ceb.2012.08.008.'
short: J.S. Gomez-Cavazos, M. Hetzer, Current Opinion in Cell Biology 24 (2012)
775–783.
date_created: 2022-04-07T07:51:37Z
date_published: 2012-12-01T00:00:00Z
date_updated: 2024-10-14T11:25:04Z
day: '01'
doi: 10.1016/j.ceb.2012.08.008
extern: '1'
external_id:
pmid:
- '22995343'
intvolume: ' 24'
issue: '6'
keyword:
- Cell Biology
language:
- iso: eng
month: '12'
oa_version: None
page: 775-783
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: 'Outfits for different occasions: tissue-specific roles of Nuclear Envelope
proteins'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 24
year: '2012'
...
---
_id: '11091'
abstract:
- lang: eng
text: Neoplastic cells are often characterized by specific morphological abnormalities
of the nuclear envelope (NE), which have been used for cancer diagnosis for more
than a century. The NE is a double phospholipid bilayer that encapsulates the
nuclear genome, regulates all nuclear trafficking of RNAs and proteins and prevents
the passive diffusion of macromolecules between the nucleoplasm and the cytoplasm.
Whether there is a consequence to the proper functioning of the cell and loss
of structural integrity of the nucleus remains unclear. Using live cell imaging,
we characterize a phenomenon wherein nuclei of several proliferating human cancer
cell lines become temporarily ruptured during interphase. Strikingly, NE rupturing
was associated with the mislocalization of nucleoplasmic and cytoplasmic proteins
and, in the most extreme cases, the entrapment of cytoplasmic organelles in the
nuclear interior. In addition, we observed the formation of micronuclei-like structures
during interphase and the movement of chromatin out of the nuclear space. The
frequency of these NE rupturing events was higher in cells in which the nuclear
lamina, a network of intermediate filaments providing mechanical support to the
NE, was not properly formed. Our data uncover the existence of a NE instability
that has the potential to change the genomic landscape of cancer cells.
article_processing_charge: No
article_type: original
author:
- first_name: Jesse D.
full_name: Vargas, Jesse D.
last_name: Vargas
- first_name: Emily M.
full_name: Hatch, Emily M.
last_name: Hatch
- 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: Vargas JD, Hatch EM, Anderson DJ, Hetzer M. Transient nuclear envelope rupturing
during interphase in human cancer cells. Nucleus. 2012;3(1):88-100. doi:10.4161/nucl.18954
apa: Vargas, J. D., Hatch, E. M., Anderson, D. J., & Hetzer, M. (2012). Transient
nuclear envelope rupturing during interphase in human cancer cells. Nucleus.
Taylor & Francis. https://doi.org/10.4161/nucl.18954
chicago: Vargas, Jesse D., Emily M. Hatch, Daniel J. Anderson, and Martin Hetzer.
“Transient Nuclear Envelope Rupturing during Interphase in Human Cancer Cells.”
Nucleus. Taylor & Francis, 2012. https://doi.org/10.4161/nucl.18954.
ieee: J. D. Vargas, E. M. Hatch, D. J. Anderson, and M. Hetzer, “Transient nuclear
envelope rupturing during interphase in human cancer cells,” Nucleus, vol.
3, no. 1. Taylor & Francis, pp. 88–100, 2012.
ista: Vargas JD, Hatch EM, Anderson DJ, Hetzer M. 2012. Transient nuclear envelope
rupturing during interphase in human cancer cells. Nucleus. 3(1), 88–100.
mla: Vargas, Jesse D., et al. “Transient Nuclear Envelope Rupturing during Interphase
in Human Cancer Cells.” Nucleus, vol. 3, no. 1, Taylor & Francis, 2012,
pp. 88–100, doi:10.4161/nucl.18954.
short: J.D. Vargas, E.M. Hatch, D.J. Anderson, M. Hetzer, Nucleus 3 (2012) 88–100.
date_created: 2022-04-07T07:51:53Z
date_published: 2012-01-01T00:00:00Z
date_updated: 2024-10-14T11:25:37Z
day: '01'
doi: 10.4161/nucl.18954
extern: '1'
external_id:
pmid:
- '22567193'
intvolume: ' 3'
issue: '1'
keyword:
- Cell Biology
language:
- iso: eng
month: '01'
oa_version: None
page: 88-100
pmid: 1
publication: Nucleus
publication_identifier:
eissn:
- 1949-1042
issn:
- 1949-1034
publication_status: published
publisher: Taylor & Francis
quality_controlled: '1'
scopus_import: '1'
status: public
title: Transient nuclear envelope rupturing during interphase in human cancer cells
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 3
year: '2012'
...
---
_id: '11093'
abstract:
- lang: eng
text: Nuclear pore complexes (NPCs) are built from ∼30 different proteins called
nucleoporins or Nups. Previous studies have shown that several Nups exhibit cell-type-specific
expression and that mutations in NPC components result in tissue-specific diseases.
Here we show that a specific change in NPC composition is required for both myogenic
and neuronal differentiation. The transmembrane nucleoporin Nup210 is absent in
proliferating myoblasts and embryonic stem cells (ESCs) but becomes expressed
and incorporated into NPCs during cell differentiation. Preventing Nup210 production
by RNAi blocks myogenesis and the differentiation of ESCs into neuroprogenitors.
We found that the addition of Nup210 to NPCs does not affect nuclear transport
but is required for the induction of genes that are essential for cell differentiation.
Our results identify a single change in NPC composition as an essential step in
cell differentiation and establish a role for Nup210 in gene expression regulation
and cell fate determination.
article_processing_charge: No
article_type: original
author:
- first_name: Maximiliano A.
full_name: D'Angelo, Maximiliano A.
last_name: D'Angelo
- first_name: J. Sebastian
full_name: Gomez-Cavazos, J. Sebastian
last_name: Gomez-Cavazos
- first_name: Arianna
full_name: Mei, Arianna
last_name: Mei
- first_name: Daniel H.
full_name: Lackner, Daniel H.
last_name: Lackner
- 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, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. A change in nuclear
pore complex composition regulates cell differentiation. Developmental Cell.
2012;22(2):446-458. doi:10.1016/j.devcel.2011.11.021
apa: D’Angelo, M. A., Gomez-Cavazos, J. S., Mei, A., Lackner, D. H., & Hetzer,
M. (2012). A change in nuclear pore complex composition regulates cell differentiation.
Developmental Cell. Elsevier. https://doi.org/10.1016/j.devcel.2011.11.021
chicago: D’Angelo, Maximiliano A., J. Sebastian Gomez-Cavazos, Arianna Mei, Daniel H.
Lackner, and Martin Hetzer. “A Change in Nuclear Pore Complex Composition Regulates
Cell Differentiation.” Developmental Cell. Elsevier, 2012. https://doi.org/10.1016/j.devcel.2011.11.021.
ieee: M. A. D’Angelo, J. S. Gomez-Cavazos, A. Mei, D. H. Lackner, and M. Hetzer,
“A change in nuclear pore complex composition regulates cell differentiation,”
Developmental Cell, vol. 22, no. 2. Elsevier, pp. 446–458, 2012.
ista: D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. 2012. A change
in nuclear pore complex composition regulates cell differentiation. Developmental
Cell. 22(2), 446–458.
mla: D’Angelo, Maximiliano A., et al. “A Change in Nuclear Pore Complex Composition
Regulates Cell Differentiation.” Developmental Cell, vol. 22, no. 2, Elsevier,
2012, pp. 446–58, doi:10.1016/j.devcel.2011.11.021.
short: M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental
Cell 22 (2012) 446–458.
date_created: 2022-04-07T07:52:10Z
date_published: 2012-01-19T00:00:00Z
date_updated: 2024-10-14T11:26:00Z
day: '19'
doi: 10.1016/j.devcel.2011.11.021
extern: '1'
external_id:
pmid:
- '22264802'
intvolume: ' 22'
issue: '2'
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.2011.11.021
month: '01'
oa: 1
oa_version: Published Version
page: 446-458
pmid: 1
publication: Developmental Cell
publication_identifier:
issn:
- 1534-5807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: A change in nuclear pore complex composition regulates cell differentiation
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 22
year: '2012'
...
---
_id: '11094'
abstract:
- lang: eng
text: Nuclear pore complexes (NPCs) assemble at the end of mitosis during nuclear
envelope (NE) reformation and into an intact NE as cells progress through interphase.
Although recent studies have shown that NPC formation occurs by two different
molecular mechanisms at two distinct cell cycle stages, little is known about
the molecular players that mediate the fusion of the outer and inner nuclear membranes
to form pores. In this paper, we provide evidence that the transmembrane nucleoporin
(Nup), POM121, but not the Nup107–160 complex, is present at new pore assembly
sites at a time that coincides with inner nuclear membrane (INM) and outer nuclear
membrane (ONM) fusion. Overexpression of POM121 resulted in juxtaposition of the
INM and ONM. Additionally, Sun1, an INM protein that is known to interact with
the cytoskeleton, was specifically required for interphase assembly and localized
with POM121 at forming pores. We propose a model in which POM121 and Sun1 interact
transiently to promote early steps of interphase NPC assembly.
article_processing_charge: No
article_type: original
author:
- first_name: Jessica A.
full_name: Talamas, Jessica A.
last_name: Talamas
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Talamas JA, Hetzer M. POM121 and Sun1 play a role in early steps of interphase
NPC assembly. Journal of Cell Biology. 2011;194(1):27-37. doi:10.1083/jcb.201012154
apa: Talamas, J. A., & Hetzer, M. (2011). POM121 and Sun1 play a role in early
steps of interphase NPC assembly. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.201012154
chicago: Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in
Early Steps of Interphase NPC Assembly.” Journal of Cell Biology. Rockefeller
University Press, 2011. https://doi.org/10.1083/jcb.201012154.
ieee: J. A. Talamas and M. Hetzer, “POM121 and Sun1 play a role in early steps of
interphase NPC assembly,” Journal of Cell Biology, vol. 194, no. 1. Rockefeller
University Press, pp. 27–37, 2011.
ista: Talamas JA, Hetzer M. 2011. POM121 and Sun1 play a role in early steps of
interphase NPC assembly. Journal of Cell Biology. 194(1), 27–37.
mla: Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early
Steps of Interphase NPC Assembly.” Journal of Cell Biology, vol. 194, no.
1, Rockefeller University Press, 2011, pp. 27–37, doi:10.1083/jcb.201012154.
short: J.A. Talamas, M. Hetzer, Journal of Cell Biology 194 (2011) 27–37.
date_created: 2022-04-07T07:52:18Z
date_published: 2011-07-04T00:00:00Z
date_updated: 2024-10-14T11:26:10Z
day: '04'
doi: 10.1083/jcb.201012154
extern: '1'
external_id:
pmid:
- '21727197'
intvolume: ' 194'
issue: '1'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.201012154
month: '07'
oa: 1
oa_version: Published Version
page: 27-37
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: POM121 and Sun1 play a role in early steps of interphase NPC assembly
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 194
year: '2011'
...
---
_id: '11095'
article_processing_charge: No
article_type: letter_note
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: Giacomo
full_name: Cavalli, Giacomo
last_name: Cavalli
citation:
ama: Hetzer M, Cavalli G. Editorial overview. Current Opinion in Cell Biology.
2011;23(3):255-257. doi:10.1016/j.ceb.2011.04.013
apa: Hetzer, M., & Cavalli, G. (2011). Editorial overview. Current Opinion
in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2011.04.013
chicago: Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” Current Opinion
in Cell Biology. Elsevier, 2011. https://doi.org/10.1016/j.ceb.2011.04.013.
ieee: M. Hetzer and G. Cavalli, “Editorial overview,” Current Opinion in Cell
Biology, vol. 23, no. 3. Elsevier, pp. 255–257, 2011.
ista: Hetzer M, Cavalli G. 2011. Editorial overview. Current Opinion in Cell Biology.
23(3), 255–257.
mla: Hetzer, Martin, and Giacomo Cavalli. “Editorial Overview.” Current Opinion
in Cell Biology, vol. 23, no. 3, Elsevier, 2011, pp. 255–57, doi:10.1016/j.ceb.2011.04.013.
short: M. Hetzer, G. Cavalli, Current Opinion in Cell Biology 23 (2011) 255–257.
date_created: 2022-04-07T07:52:27Z
date_published: 2011-06-01T00:00:00Z
date_updated: 2024-10-14T11:26:20Z
day: '01'
doi: 10.1016/j.ceb.2011.04.013
extern: '1'
external_id:
pmid:
- '21592757'
intvolume: ' 23'
issue: '3'
keyword:
- Cell Biology
language:
- iso: eng
month: '06'
oa_version: None
page: 255-257
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: Editorial overview
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2011'
...
---
_id: '11096'
abstract:
- lang: eng
text: As the gatekeepers of the eukaryotic cell nucleus, nuclear pore complexes
(NPCs) mediate all molecular trafficking between the nucleoplasm and the cytoplasm.
In recent years, transport-independent functions of NPC components, nucleoporins,
have been identified including roles in chromatin organization and gene regulation.
Here, we summarize our current view of the NPC as a dynamic hub for the integration
of chromatin regulation and nuclear trafficking and discuss the functional interplay
between nucleoporins and the nuclear genome.
article_processing_charge: No
article_type: original
author:
- first_name: Yun
full_name: Liang, Yun
last_name: Liang
- 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: Liang Y, Hetzer M. Functional interactions between nucleoporins and chromatin.
Current Opinion in Cell Biology. 2011;23(1):65-70. doi:10.1016/j.ceb.2010.09.008
apa: Liang, Y., & Hetzer, M. (2011). Functional interactions between nucleoporins
and chromatin. Current Opinion in Cell Biology. Elsevier. https://doi.org/10.1016/j.ceb.2010.09.008
chicago: Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins
and Chromatin.” Current Opinion in Cell Biology. Elsevier, 2011. https://doi.org/10.1016/j.ceb.2010.09.008.
ieee: Y. Liang and M. Hetzer, “Functional interactions between nucleoporins and
chromatin,” Current Opinion in Cell Biology, vol. 23, no. 1. Elsevier,
pp. 65–70, 2011.
ista: Liang Y, Hetzer M. 2011. Functional interactions between nucleoporins and
chromatin. Current Opinion in Cell Biology. 23(1), 65–70.
mla: Liang, Yun, and Martin Hetzer. “Functional Interactions between Nucleoporins
and Chromatin.” Current Opinion in Cell Biology, vol. 23, no. 1, Elsevier,
2011, pp. 65–70, doi:10.1016/j.ceb.2010.09.008.
short: Y. Liang, M. Hetzer, Current Opinion in Cell Biology 23 (2011) 65–70.
date_created: 2022-04-07T07:52:37Z
date_published: 2011-02-01T00:00:00Z
date_updated: 2024-10-14T11:26:31Z
day: '01'
doi: 10.1016/j.ceb.2010.09.008
extern: '1'
external_id:
pmid:
- '21030234'
intvolume: ' 23'
issue: '1'
keyword:
- Cell Biology
language:
- iso: eng
month: '02'
oa_version: None
page: 65-70
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: Functional interactions between nucleoporins and chromatin
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2011'
...
---
_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: 2024-10-14T11:26:51Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: '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: 2024-10-14T11:28:25Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: 2024-10-14T11:28:48Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: 2024-10-14T11:29:10Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: 2024-10-14T11:29:21Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: 2024-10-14T11:29:29Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: 2024-10-14T11:29:38Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: 2024-10-14T11:29:47Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 121
year: '2008'
...