The COPI Complex Functions in Nuclear Envelope Breakdown and Is Recruited by the Nucleoporin Nup153

Nuclear envelope breakdown is a critical step in the cell cycle of higher eukaryotes. Although integral membrane proteins associated with the nuclear membrane have been observed to disperse into the endoplasmic reticulum at mitosis, the mechanisms involved in this reorganization remain to be fully e...

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Bibliographic Details
Published in:Developmental cell 2003-09, Vol.5 (3), p.487-498
Main Authors: Liu, Jin, Prunuske, Amy J, Fager, Ammon M, Ullman, Katharine S
Format: Article
Language:English
Subjects:
ADP-Ribosylation Factors - metabolism
Animals
Blotting, Western
Cell Cycle - physiology
Coat Protein Complex I - physiology
Coatomer Protein - metabolism
Cyclins - metabolism
HeLa Cells - metabolism
Humans
Immunohistochemistry
In Vitro Techniques
Lamins - metabolism
Microscopy, Confocal
Nuclear Envelope - physiology
Nuclear Pore Complex Proteins - physiology
Ovum
Peptide Fragments
Precipitin Tests
Recombinant Proteins - chemistry
Silver Staining
Xenopus
Zinc Fingers - physiology
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Summary:Nuclear envelope breakdown is a critical step in the cell cycle of higher eukaryotes. Although integral membrane proteins associated with the nuclear membrane have been observed to disperse into the endoplasmic reticulum at mitosis, the mechanisms involved in this reorganization remain to be fully elucidated. Here, using Xenopus extracts, we report a role for the COPI coatomer complex in nuclear envelope breakdown, implicating vesiculation as an important step. We have found that a nuclear pore protein, Nup153, plays a critical role in directing COPI to the nuclear membrane at mitosis and that this event provides feedback to other aspects of nuclear disassembly. These results provide insight into how key steps in nuclear division are orchestrated.
ISSN:1534-5807
1878-1551
DOI:10.1016/S1534-5807(03)00262-4