Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin

Guillermo Velasco; Chris Armstrong; Nick Morrice; Sheelagh Frame; Philip Cohen

doi:10.1016/S0014-5793(02)03175-7

Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin

Guillermo Velasco, Chris Armstrong, Nick Morrice, Sheelagh Frame, Philip Cohen

Research output: Contribution to journal › Article › peer-review

184 Citations (Scopus)

Abstract

Rho kinase is known to control smooth muscle contractility by phosphorylating the 110 kDa myosin-targetting subunit (MYPT1) of the myosin-associated form of protein phosphatase 1 (PP1M). Phosphorylation of MYPT1 at Thr695 has previously been reported to inhibit the catalytic activity of PP1. Here, we show that the phosphorylation of Thr850 by Rho kinase dissociates PP1M from myosin, providing a second mechanism by which myosin phosphatase activity is inhibited.

Original language	English
Pages (from-to)	101-104
Number of pages	4
Journal	FEBS Letters
Volume	527
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(02)03175-7
Publication status	Published - 11 Sept 2002

Keywords

Myosin
Protein phosphatase 1
Rho kinase
Smooth muscle

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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AU - Velasco, Guillermo

AU - Armstrong, Chris

AU - Morrice, Nick

AU - Frame, Sheelagh

AU - Cohen, Philip

PY - 2002/9/11

Y1 - 2002/9/11

N2 - Rho kinase is known to control smooth muscle contractility by phosphorylating the 110 kDa myosin-targetting subunit (MYPT1) of the myosin-associated form of protein phosphatase 1 (PP1M). Phosphorylation of MYPT1 at Thr695 has previously been reported to inhibit the catalytic activity of PP1. Here, we show that the phosphorylation of Thr850 by Rho kinase dissociates PP1M from myosin, providing a second mechanism by which myosin phosphatase activity is inhibited.

AB - Rho kinase is known to control smooth muscle contractility by phosphorylating the 110 kDa myosin-targetting subunit (MYPT1) of the myosin-associated form of protein phosphatase 1 (PP1M). Phosphorylation of MYPT1 at Thr695 has previously been reported to inhibit the catalytic activity of PP1. Here, we show that the phosphorylation of Thr850 by Rho kinase dissociates PP1M from myosin, providing a second mechanism by which myosin phosphatase activity is inhibited.

KW - Myosin

KW - Protein phosphatase 1

KW - Rho kinase

KW - Smooth muscle

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Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin

Abstract

Keywords

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