Myosin phosphatase dephosphorylates PLK1

Stable Identifier
Reaction [transition]
Homo sapiens
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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).

Literature References
PubMed ID Title Journal Year
22641346 LATS1/WARTS phosphorylates MYPT1 to counteract PLK1 and regulate mammalian mitotic progression

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

J. Cell Biol. 2012
22365832 Plk1-dependent phosphorylation of optineurin provides a negative feedback mechanism for mitotic progression

Laplantine, E, Bennett, KL, Superti-Furga, G, Weil, R, Kachaner, D, Israel, A, Bauch, A, Filipe, J

Mol. Cell 2012
18477460 Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1

Goto, H, Kaibuchi, K, Hartshorne, DJ, Totsukawa, G, Matsumura, F, Yamashiro, S, Ito, M, Yamakita, Y

Dev. Cell 2008
Catalyst Activity

protein serine/threonine phosphatase activity of Phosphorylated Myosin Phosphatase [nucleoplasm]

This event is regulated