Cyclin E/A:Cdk2-mediated phosphorylation of p27/p21

Stable Identifier
R-HSA-187520
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

The interaction between the Skp2 subunit of the SCF(Skp2) complex and p27 is dependent upon Cdk2:Cyclin A/E mediated phosphorylation of p27 at Thr 187 (Carrano et al, 1999; Tsvetkov et al, 1999). There is evidence that Cyclin A/B:Cdk1 can also bind and phosphorylate p27 on Thr 187 (Nakayama et al., 2004). This phosphorylation is also essential for the subsequent ubiquitination of p27.

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
10559916 SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27

Carrano, AC, Eytan, E, Hershko, A, Pagano, M

Nat Cell Biol 1999
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 Cyclin E/A:p-T160-CDK2:CDKN1A,CDKN1B [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed