PPM1D dephosphorylates RUNX2

Stable Identifier
Homo sapiens
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PPM1D (Wip1), a serine/threonine phosphatase, dephosphorylates RUNX2 on serine residue S432. Since it has not been tested whether S432 affects bindng of RUNX2 to CBFB, PPM1D is shown to dephosphorylate RUNX2 in the context of its complex with CBFB. The kinase responsible for RUNX2 phosphorylation at S432 is not known. PPM1D-mediated dephosphorylation of RUNX2 promotes RUNX2-mediated transcriptional activation of BAX and may play an important role in inducing apoptosis in TP53 negative tumor cells (Goloudina, Tanoue et al. 2012, Goloudina, Mazur et al. 2012).

Literature References
PubMed ID Title Journal Year
22065775 Wip1 promotes RUNX2-dependent apoptosis in p53-negative tumors and protects normal tissues during treatment with anticancer agents

Hammann, A, Garrido, C, Goloudina, AR, Bulavin, DV, Appella, E, Tanoue, K, le Guezennec, X, Demidov, ON, Fourmaux, E, Mazur, SJ

Proc. Natl. Acad. Sci. U.S.A. 2012
22544321 Wip1 sensitizes p53-negative tumors to apoptosis by regulating the Bax/Bcl-xL ratio

Garrido, C, Goloudina, AR, Appella, E, Demidov, ON, Mazur, SJ

Cell Cycle 2012
Catalyst Activity

protein serine/threonine kinase activity of PPM1D [nucleoplasm]

Orthologous Events
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