2.50
Hdl Handle:
http://hdl.handle.net/10541/70384
Title:
Nuclear membrane disassembly and rupture.
Authors:
Cotter, Laura A; Allen, Terence D; Kiseleva, Elena; Goldberg, Martin W
Abstract:
The nuclear envelope consists of two membranes traversed by nuclear pore complexes. The outer membrane is continuous with the endoplasmic reticulum. At mitosis nuclear pore complexes are dismantled and membranes disperse. The mechanism of dispersal is controversial: one view is that membranes feed into the endoplasmic reticulum, another is that they vesiculate. Using Xenopus egg extracts, nuclei have been assembled and then induced to breakdown by addition of metaphase extract. Field emission scanning electron microscopy was used to study disassembly. Strikingly, endoplasmic reticulum-like membrane tubules form from the nuclear surface after the addition of metaphase extracts, but vesicles were also observed. Microtubule inhibitors slowed but did not prevent membrane removal, whereas Brefeldin A, which inhibits vesicle formation, stops membrane disassembly, suggesting that vesiculation is necessary. Structures that looked like coated buds were observed and buds were labelled for beta-COP. We show that nuclear pore complexes are dismantled and the pore closed prior to membrane rupturing, suggesting that rupturing is an active process rather than a result of enlargement of nuclear pores.
Affiliation:
Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Wilmslow Road, Manchester M20 4BX, UK.
Citation:
Nuclear membrane disassembly and rupture. 2007, 369 (3):683-95 J. Mol. Biol.
Journal:
Journal of Molecular Biology
Issue Date:
8-Jun-2007
URI:
http://hdl.handle.net/10541/70384
DOI:
10.1016/j.jmb.2007.03.051
PubMed ID:
17467734
Type:
Article
Language:
en
ISSN:
0022-2836
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorCotter, Laura A-
dc.contributor.authorAllen, Terence D-
dc.contributor.authorKiseleva, Elena-
dc.contributor.authorGoldberg, Martin W-
dc.date.accessioned2009-06-12T15:13:10Z-
dc.date.available2009-06-12T15:13:10Z-
dc.date.issued2007-06-08-
dc.identifier.citationNuclear membrane disassembly and rupture. 2007, 369 (3):683-95 J. Mol. Biol.en
dc.identifier.issn0022-2836-
dc.identifier.pmid17467734-
dc.identifier.doi10.1016/j.jmb.2007.03.051-
dc.identifier.urihttp://hdl.handle.net/10541/70384-
dc.description.abstractThe nuclear envelope consists of two membranes traversed by nuclear pore complexes. The outer membrane is continuous with the endoplasmic reticulum. At mitosis nuclear pore complexes are dismantled and membranes disperse. The mechanism of dispersal is controversial: one view is that membranes feed into the endoplasmic reticulum, another is that they vesiculate. Using Xenopus egg extracts, nuclei have been assembled and then induced to breakdown by addition of metaphase extract. Field emission scanning electron microscopy was used to study disassembly. Strikingly, endoplasmic reticulum-like membrane tubules form from the nuclear surface after the addition of metaphase extracts, but vesicles were also observed. Microtubule inhibitors slowed but did not prevent membrane removal, whereas Brefeldin A, which inhibits vesicle formation, stops membrane disassembly, suggesting that vesiculation is necessary. Structures that looked like coated buds were observed and buds were labelled for beta-COP. We show that nuclear pore complexes are dismantled and the pore closed prior to membrane rupturing, suggesting that rupturing is an active process rather than a result of enlargement of nuclear pores.en
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshBrefeldin A-
dc.subject.meshCell Membrane-
dc.subject.meshCell Nucleus-
dc.subject.meshCoatomer Protein-
dc.subject.meshEndoplasmic Reticulum-
dc.subject.meshGuanosine 5'-O-(3-Thiotriphosphate)-
dc.subject.meshImmunohistochemistry-
dc.subject.meshMetaphase-
dc.subject.meshMicrotubules-
dc.subject.meshMitosis-
dc.subject.meshModels, Biological-
dc.subject.meshNuclear Envelope-
dc.subject.meshNuclear Pore-
dc.subject.meshXenopus-
dc.titleNuclear membrane disassembly and rupture.en
dc.typeArticleen
dc.contributor.departmentPaterson Institute for Cancer Research, Christie Hospital NHS Trust, Wilmslow Road, Manchester M20 4BX, UK.en
dc.identifier.journalJournal of Molecular Biologyen

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