The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153. Dev Cell 2003 Sep;5(3):487-98
Date
09/12/2003Pubmed ID
12967567DOI
10.1016/s1534-5807(03)00262-4Scopus ID
2-s2.0-0042196107 (requires institutional sign-in at Scopus site) 63 CitationsAbstract
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 KSAuthor
Amy Jeanette Prunuske PhD Professor in the Medical School Regional Campuses department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ADP-Ribosylation FactorsAnimals
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
