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Acetylation of cyclin A: a new cell cycle regulatory mechanism

Authors :
Maria Jesús Pujol
Oriol Bachs
Francesca Mateo
Miriam Vidal-Laliena
Source :
Biochemical Society transactions. 38(Pt 1)
Publication Year :
2010

Abstract

Cyclin A must be degraded at prometaphase in order to allow mitosis progression. Nevertheless, the signals that trigger cyclin A degradation at mitosis have been largely elusive. In the present paper, we review the status of cyclin A degradation in the light of recent evidence indicating that acetylation plays a role in cyclin A stability. The emerging model proposes that the acetyltransferase PCAF [p300/CREB (cAMP-response-element-binding protein)-binding protein-associated factor] [perhaps also its homologue GCN5 (general control non-derepressible 5)] acetylates cyclin A at Lys54, Lys68, Lys95 and Lys112 during mitosis, leading to its ubiquitylation by the anaphase-promoting factor/cyclosome and its subsequent degradation via proteasome. Interestingly, these four lysine residues in cyclin A also participate in the regulation of cyclin A–Cdk (cyclin-dependent kinase) activity by modulating its interaction with Cdks.

Details

ISSN :
14708752
Volume :
38
Issue :
Pt 1
Database :
OpenAIRE
Journal :
Biochemical Society transactions
Accession number :
edsair.doi.dedup.....15f83243d07b82a1e728f61e70d3fc9d