Author
Listed:
- Vincenzo D’Angiolella
(NYU Cancer Institute, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, New York 10016, USA)
- Valerio Donato
(NYU Cancer Institute, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, New York 10016, USA)
- Sangeetha Vijayakumar
(NYU Cancer Institute, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, New York 10016, USA)
- Anita Saraf
(The Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, Missouri 64110, USA)
- Laurence Florens
(The Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, Missouri 64110, USA)
- Michael P. Washburn
(The Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, Missouri 64110, USA
The University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, Kansas 66160, USA)
- Brian Dynlacht
(NYU Cancer Institute, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, New York 10016, USA)
- Michele Pagano
(NYU Cancer Institute, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, New York 10016, USA
Howard Hughes Medical Institute)
Abstract
A role for Cyclin F Cyclin F is the founding member of the F-box protein family but its functions are unknown. In contrast to most cyclins, it does not bind or activate cyclin-dependent kinases (CDKs). Here, a protein essential for centrosome duplication, CP110, is identified as a substrate of Cyclin F. CP110 and Cyclin F associate on centrioles during the cell cycle, and Cyclin F is proposed to limit centrosome duplication by targeting CP110 for degradation.
Suggested Citation
Vincenzo D’Angiolella & Valerio Donato & Sangeetha Vijayakumar & Anita Saraf & Laurence Florens & Michael P. Washburn & Brian Dynlacht & Michele Pagano, 2010.
"SCFCyclin F controls centrosome homeostasis and mitotic fidelity through CP110 degradation,"
Nature, Nature, vol. 466(7302), pages 138-142, July.
Handle:
RePEc:nat:nature:v:466:y:2010:i:7302:d:10.1038_nature09140
DOI: 10.1038/nature09140
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