Description: The docking sites for PP1 (e.g. Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA)) and Cdk-Cyclins (e.g. Cyclin-A2 (CCNA2)) on Retinoblastoma-associated protein (RB1) overlap, which makes their binding to RB1 mutually exclusive. Hypophosphorylated RB1 blocks E2F-dependent transcription, while hyperphosphorylation inactivates RB1 as a repressor, thereby promoting cell cycle progression.
Participants: (1) Retinoblastoma-associated protein (RB1) (2) Cyclin-A2 (CCNA2) (3) Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (PPP1CA)
(1) An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein.Hirschi et al. Nat. Struct. Mol. Biol. (2010)
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