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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Format: | Journal article |
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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. |
first_indexed | 2024-03-07T06:50:20Z |
format | Journal article |
id | oxford-uuid:fc599f68-30cb-473a-9740-2faf50635a73 |
institution | University of Oxford |
last_indexed | 2024-03-07T06:50:20Z |
publishDate | 2013 |
record_format | dspace |
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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