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).
Qiao, M, Passaniti, A, Shapiro, P, Kumar, R, Fosbrink, M, Rus, H
van Wijnen, AJ, Rajgopal, A, Lian, JB, Stein, JL, Mujeeb, KA, Stein, GS, Young, DW
cyclin-dependent protein serine/threonine kinase activity of CCNB1:p-T161-CDK1 [nucleoplasm]
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