A Caltech Library Service

Cyclin F Is Degraded during G2-M by Mechanisms Fundamentally Different from Other Cyclins

Fung, Tsz Kan and Siu, Wai Yi and Yam, Cain H. and Lau, Anita and Poon, Randy Y. C. (2002) Cyclin F Is Degraded during G2-M by Mechanisms Fundamentally Different from Other Cyclins. Journal of Biological Chemistry, 277 (38). pp. 35140-35149. ISSN 0021-9258. doi:10.1074/jbc.M205503200.

PDF - Published Version
See Usage Policy.


Use this Persistent URL to link to this item:


Cyclin F, a cyclin that can form SCF complexes and bind to cyclin B, oscillates in the cell cycle with a pattern similar to cyclin A and cyclin B. Ectopic expression of cyclin F arrests the cell cycle in G2/M. How the level of cyclin F is regulated during the cell cycle is completely obscure. Here we show that, similar to cyclin A, cyclin F is degraded when the spindle assembly checkpoint is activated and accumulates when the DNA damage checkpoint is activated. Cyclin F is a very unstable protein throughout much of the cell cycle. Unlike other cyclins, degradation of cyclin F is independent of ubiquitination and proteasome-mediated pathways. Interestingly, proteolysis of cyclin F is likely to involve metalloproteases. Rapid destruction of cyclin F does not require the N-terminal F-box motif but requires the COOH-terminal PEST sequences. The PEST region alone is sufficient to interfere with the degradation of cyclin F and confer instability when fused to cyclin A. These data show that although cyclin F is degraded at similar time as the mitotic cyclins, the underlying mechanisms are entirely distinct.

Item Type:Article
Related URLs:
URLURL TypeDescription
Additional Information:© 2002 The American Society for Biochemistry and Molecular Biology, Inc. Received for publication, June 4, 2002, and in revised form, July 16, 2002. Originally published In Press as doi:10.1074/jbc.M205503200 on July 16, 2002. We are grateful for Dr. Tim Hunt for generous gifts of reagents. Many thanks are due to members of the Poon laboratory for technical assistance and comments on the manuscript. This work was supported in part by awards and grants from the Croucher Foundation, the Philip Morris External Research Program, and Research Grants Council Grant HKUST6194/99 M (to R. Y. C. P.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Issue or Number:38
Record Number:CaltechAUTHORS:FUNjbc02
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:3379
Deposited By: Archive Administrator
Deposited On:02 Jun 2006
Last Modified:08 Nov 2021 19:55

Repository Staff Only: item control page