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    Nuclear membrane disassembly and rupture.

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    Authors
    Cotter, Laura A
    Allen, Terence D
    Kiseleva, Elena
    Goldberg, Martin W
    Affiliation
    Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Wilmslow Road, Manchester M20 4BX, UK.
    Issue Date
    2007-06-08
    
    Metadata
    Show full item record
    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.
    Citation
    Nuclear membrane disassembly and rupture. 2007, 369 (3):683-95 J. Mol. Biol.
    Journal
    Journal of Molecular Biology
    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
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.jmb.2007.03.051
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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