---
_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: 2024-10-14T11:30:08Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: 2024-10-14T11:30:38Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: '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
license: https://creativecommons.org/licenses/by/4.0/
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: '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: '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'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/S1097-2765(00)80266-X
month: '06'
oa: 1
oa_version: Published Version
page: 1013-1024
pmid: 1
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
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'
...