Phosphorylation of proteins involved in the G1/S transition by Cyclin A:Cdk2

Stable Identifier
R-HSA-187948
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Active Cyclin A:Cdk2 complexes phosphorylate and inactivate proteins required for maintaining the G1/S phase including. In addition to CDKN1A and CDKN1B, the active CCNA:p-T160-CDK2 complex also phosphorylates FZR1 (Cdh1) and RB1. All this creates auto-amplification loops that render Cdk2 increasingly more active. In G2, Cdk2, in association with cyclin A, phosphorylates E2F1 and E2F3 resulting in the inactivation and possibly degradation of these two transcription factors (Dynlacht et al., 1994; Krek et al., 1994).

Literature References
PubMed ID Title Journal Year
10323868 Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation

Montagnoli, A, Fiore, F, Eytan, E, Carrano, AC, Draetta, GF, Hershko, A, Pagano, M

Genes Dev 1999
12730199 Role of the SCFSkp2 ubiquitin ligase in the degradation of p21Cip1 in S phase

Bornstein, G, Bloom, J, Sitry-Shevah, D, Nakayama, K, Pagano, M, Hershko, A

J Biol Chem 2003
16582612 Dual regulation of the anaphase promoting complex in human cells by cyclin A-Cdk2 and cyclin A-Cdk1 complexes

Mitra, J, Enders, GH, Azizkhan-Clifford, J, Lengel, KL

Cell Cycle 2006
10375532 p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27

Tsvetkov, LM, Yeh, KH, Lee, SJ, Sun, H, Zhang, H

Curr Biol 1999
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
cyclin-dependent protein serine/threonine kinase activity of CCNA:p-T160-CDK2 [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created