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,...
| Main Authors: | , , |
|---|---|
| Format: | Journal article |
| Published: |
Elsevier
2012
|
| _version_ | 1797062934624468992 |
|---|---|
| author | D'Angiolella, V Esencay, M Pagano, M |
| author_facet | D'Angiolella, V Esencay, M Pagano, M |
| author_sort | D'Angiolella, V |
| collection | OXFORD |
| description | <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> |
| first_indexed | 2024-03-06T20:52:38Z |
| format | Journal article |
| id | oxford-uuid:381f2351-87e1-4e99-aba0-6130d5e828a0 |
| institution | University of Oxford |
| last_indexed | 2024-03-06T20:52:38Z |
| publishDate | 2012 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:381f2351-87e1-4e99-aba0-6130d5e828a02022-03-26T13:48:04ZA cyclin without cyclin-dependent kinases: cyclin F controls genome stability through ubiquitin-mediated proteolysisJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:381f2351-87e1-4e99-aba0-6130d5e828a0Symplectic Elements at OxfordElsevier2012D'Angiolella, VEsencay, MPagano, M <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> |
| spellingShingle | D'Angiolella, V Esencay, 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 |
| work_keys_str_mv | AT dangiolellav acyclinwithoutcyclindependentkinasescyclinfcontrolsgenomestabilitythroughubiquitinmediatedproteolysis AT esencaym acyclinwithoutcyclindependentkinasescyclinfcontrolsgenomestabilitythroughubiquitinmediatedproteolysis AT paganom acyclinwithoutcyclindependentkinasescyclinfcontrolsgenomestabilitythroughubiquitinmediatedproteolysis AT dangiolellav cyclinwithoutcyclindependentkinasescyclinfcontrolsgenomestabilitythroughubiquitinmediatedproteolysis AT esencaym cyclinwithoutcyclindependentkinasescyclinfcontrolsgenomestabilitythroughubiquitinmediatedproteolysis AT paganom cyclinwithoutcyclindependentkinasescyclinfcontrolsgenomestabilitythroughubiquitinmediatedproteolysis |