CDK1 phosphorylates RUNX2

Stable Identifier
Homo sapiens
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RUNX2, presumably in complex with CBFB, can be phosphorylated by the complex of CDK1 and cyclin B. The interaction was demonstrated between endogenous human RUNX2 and CDK1:CCNB1. It was also shown in human cells that RUNX2 undergoes CDK1:CCNB1-mediated phosphorylation on serine residue S451 of RUNX2-P2 isoform. This residue corresponds to the mouse Runx-P1 serine residue S472 (Qiao et al. 2006, Rajgopal et al. 2007). At mitotic exit, RUNX2 is dephosphorylated by unidentified PP1 or PP2A phosphatase (Rajgopal et al. 2007).

Literature References
PubMed ID Title Journal Year
16407259 Cell cycle-dependent phosphorylation of the RUNX2 transcription factor by cdc2 regulates endothelial cell proliferation

Qiao, M, Passaniti, A, Shapiro, P, Kumar, R, Fosbrink, M, Rus, H

J. Biol. Chem. 2006
17171635 Mitotic control of RUNX2 phosphorylation by both CDK1/cyclin B kinase and PP1/PP2A phosphatase in osteoblastic cells

van Wijnen, AJ, Rajgopal, A, Lian, JB, Stein, JL, Mujeeb, KA, Stein, GS, Young, DW

J. Cell. Biochem. 2007
Catalyst Activity

cyclin-dependent protein serine/threonine kinase activity of CCNB1:p-T161-CDK1 [nucleoplasm]

Orthologous Events
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