Acetylation of cyclin A: a new cell cycle regulatory mechanism.
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.
Mateo
Francesca
F
Department of Cell Biology, Immunology and Neurosciences, Faculty of Medicine, University of Barcelona, Casanova 143, 08036 Barcelona, Spain.
Vidal-Laliena
Miriam
M
Pujol
Maria Jesus
MJ
Bachs
Oriol
O
D000107:Acetylation; D002453:Cell Cycle / Q000502:physiology*; D019925:Cyclin A / Q000235:genetics / Q000378:metabolism*; D051357:Cyclin-Dependent Kinase 2 / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D009154:Mutation; D054875:Ubiquitination; D050880:p300-CBP Transcription Factors / Q000378:metabolism; D000099224:p300-CBP-Associated Factor
D019925:Cyclin A; D051357:Cyclin-Dependent Kinase 2; D008239:Lysine; D050880:p300-CBP Transcription Factors; D000099224:p300-CBP-Associated Factor