The myosin phosphatase complex can dephosphorylate PLK1 threonine residue T210 and inactivate PLK1 (Yamashiro et al. 2008). Myosin phosphatase is activated through phosphorylation of its PPP1R12A (MYPT1) subunit. Several kinases, including CDK1 (Yamashiro et al. 2008) and LATS1 (Chiyoda et al. 2012) have been implicated in myosin phosphatase activation, but the position and temporal order of key PPP1R12A phosphorylations need to be investigated further. Phosphorylated OPTN (optineurin) is able to bind PPP1R12A (MYPT1) and positively regulates PLK1 dephosphorylation by myosin phosphatase, posibly by facilitating PPP1R12A phosphorylation and myosin phosphatase activation (Kachaner et al. 2012).
Saya, H, Ishihama, Y, Ito, M, Sugiyama, N, Kuninaka, S, Arima, Y, Aoki, D, Shimizu, T, Tsuda, H, Kaibuchi, K, Naoe, H, Ishizawa, J, Chiyoda, T, Kobayashi, Y
Laplantine, E, Bennett, KL, Superti-Furga, G, Weil, R, Kachaner, D, Israel, A, Bauch, A, Filipe, J
Goto, H, Kaibuchi, K, Hartshorne, DJ, Totsukawa, G, Matsumura, F, Yamashiro, S, Ito, M, Yamakita, Y
protein serine/threonine phosphatase activity of Phosphorylated Myosin Phosphatase [nucleoplasm]
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