Acetylation of cyclin A: a new cell cycle regulatory mechanism.

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.

journal_name

Biochem Soc Trans

authors

Mateo F,Vidal-Laliena M,Pujol MJ,Bachs O

doi

10.1042/BST0380083

subject

Has Abstract

pub_date

2010-02-01 00:00:00

pages

83-6

issue

Pt 1

eissn

0300-5127

issn

1470-8752

pii

BST0380083

journal_volume

38

pub_type

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