A cyclin without cyclin-dependent kinases: cyclin F controls genome stability through ubiquitin-mediated proteolysis

<p style="text-align:justify;"> Cell cycle transitions are driven by the periodic oscillations of cyclins, which bind and activate cyclin-dependent kinases (CDKs) to phosphorylate target substrates. Cyclin F uses a substrate recruitment strategy similar to that of the other cyclins,...

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Bibliographic Details
Main Authors: D'Angiolella, V, Esencay, M, Pagano, M
Format: Journal article
Published: Elsevier 2012
Description
Summary:<p style="text-align:justify;"> Cell cycle transitions are driven by the periodic oscillations of cyclins, which bind and activate cyclin-dependent kinases (CDKs) to phosphorylate target substrates. Cyclin F uses a substrate recruitment strategy similar to that of the other cyclins, but its associated catalytic activity is substantially different. Indeed, cyclin F is the founding member of the F-box family of proteins, which are the substrate recognition subunits of Skp1-Cul1-F-box protein (SCF) ubiquitin ligase complexes. Here, we discuss cyclin F function and recently identified substrates of SCFcyclin F involved in deoxyribonucleotide triphosphate (dNTP) production, centrosome duplication, and spindle formation. We highlight the relevance of cyclin F in controlling genome stability through ubiquitin-mediated proteolysis and the implications for cancer development. </p>