Reactome | Myosin phosphatase dephosphorylates PLK1

Myosin phosphatase dephosphorylates PLK1

Stable Identifier

R-HSA-3002811

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Myosin phosphatase dephosphorylates PLK1

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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 Chiyoda, T, Sugiyama, N, Shimizu, T, Naoe, H, Kobayashi, Y, Ishizawa, J, Arima, Y, Tsuda, H, Ito, M, Kaibuchi, K, Aoki, D, Ishihama, Y, Saya, H, Kuninaka, S	J. Cell Biol.	2012
22365832	Plk1-dependent phosphorylation of optineurin provides a negative feedback mechanism for mitotic progression Kachaner, D, Filipe, J, Laplantine, E, Bauch, A, Bennett, KL, Superti-Furga, G, Israel, A, Weil, R	Mol. Cell	2012
18477460	Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1 Yamashiro, S, Yamakita, Y, Totsukawa, G, Goto, H, Kaibuchi, K, Ito, M, Hartshorne, DJ, Matsumura, F	Dev. Cell	2008