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The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153. Dev Cell 2003 Sep;5(3):487-98

Date

09/12/2003

Pubmed ID

12967567

DOI

10.1016/s1534-5807(03)00262-4

Abstract

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.

Author List

Liu J, Prunuske AJ, Fager AM, Ullman KS

Author

Amy Jeanette Prunuske PhD Associate Professor in the Medical School Regional Campuses department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

ADP-Ribosylation Factors
Animals
Blotting, Western
Cell Cycle
Coat Protein Complex I
Coatomer Protein
Cyclins
HeLa Cells
Humans
Immunohistochemistry
In Vitro Techniques
Lamins
Microscopy, Confocal
Nuclear Envelope
Nuclear Pore Complex Proteins
Ovum
Peptide Fragments
Precipitin Tests
Recombinant Proteins
Silver Staining
Xenopus
Zinc Fingers
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a