Acetylation of cyclin A: a new cell cycle regulatory mechanism. (19th January 2010)

• Record Type: Journal Article
• Authors: Mateo, Francesca; Vidal-Laliena, Miriam; Pujol, Maria Jesus; Bachs, Oriol
• Is Part Of: Biochemical Society transactions. Volume 38:Number 1(2010)
• Page Start: 83
• Page End: 86
• Publication Date: 2010-01-19
• Subjects: acetylation -- cAMP-response-element-binding protein (CREB) -- p300/CREB-binding protein-associated factor (PCAF) -- cyclin A -- degradation -- ubiquitylation; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0380083
• Languages: English
• ISSNs: 0300-5127

Abstract

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 Lys 54, Lys 68, Lys 95 and Lys 112 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.