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

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 substan...

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Main Authors: D'Angiolella, V, Esencay, M, Pagano, M
Format: Journal article
Published: 2013
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author D'Angiolella, V
Esencay, M
Pagano, M
Pagano, M
author_facet D'Angiolella, V
Esencay, M
Pagano, M
Pagano, M
author_sort D'Angiolella, V
collection OXFORD
description 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. © 2012 Elsevier Ltd.
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spelling oxford-uuid:fc599f68-30cb-473a-9740-2faf50635a732022-03-27T13:19:58ZA cyclin without cyclin-dependent kinases: Cyclin F controls genome stability through ubiquitin-mediated proteolysisJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:fc599f68-30cb-473a-9740-2faf50635a73Symplectic Elements at Oxford2013D'Angiolella, VEsencay, MPagano, MPagano, MCell 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. © 2012 Elsevier Ltd.
spellingShingle D'Angiolella, V
Esencay, M
Pagano, M
Pagano, M
A cyclin without cyclin-dependent kinases: Cyclin F controls genome stability through ubiquitin-mediated proteolysis
title A cyclin without cyclin-dependent kinases: Cyclin F controls genome stability through ubiquitin-mediated proteolysis
title_full A cyclin without cyclin-dependent kinases: Cyclin F controls genome stability through ubiquitin-mediated proteolysis
title_fullStr A cyclin without cyclin-dependent kinases: Cyclin F controls genome stability through ubiquitin-mediated proteolysis
title_full_unstemmed A cyclin without cyclin-dependent kinases: Cyclin F controls genome stability through ubiquitin-mediated proteolysis
title_short A cyclin without cyclin-dependent kinases: Cyclin F controls genome stability through ubiquitin-mediated proteolysis
title_sort cyclin without cyclin dependent kinases cyclin f controls genome stability through ubiquitin mediated proteolysis
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