RB1 recruits APC/C:Cdh1 complex to SKP2

Stable Identifier
Reaction [binding]
Homo sapiens
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The pocket domain of the RB1 tumor suppressor protein binds to the N-terminal domain of SKP2, a component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex, whose targets include the cyclin-dependent kinase (CDK) inhibitor p27Kip1 (CDKN1B) (Ji et al. 2004, Binne et al. 2007). RB1 is able to simultanously interact with SKP2 and with FZR1 (Cdh1). FZR1 is a substrate-specific adapter for the anaphase promoting complex/cyclosome (APC/C). The interaction with FZR1 involves a different subregion of the pocket domain than the interaction with SKP2, and is partially dependent on the LxCxE binding cleft (Binne et al. 2007).

Literature References
PubMed ID Title Journal Year
15469821 An Rb-Skp2-p27 pathway mediates acute cell cycle inhibition by Rb and is retained in a partial-penetrance Rb mutant

Ji, P, Rekhtman, K, Pagano, M, Bloom, J, Jiang, H, Zhu, L, Ichetovkin, M

Mol. Cell 2004
17187060 Retinoblastoma protein and anaphase-promoting complex physically interact and functionally cooperate during cell-cycle exit

Binné, UK, Kaelin, WG, Rape, M, Classon, MK, Wei, W, Dyson, NJ, Dick, FA, Näär, AM

Nat. Cell Biol. 2007
Orthologous Events
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