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

FEBS Lett. 2002 Sep 11;527(1-3):101-4. doi: 10.1016/s0014-5793(02)03175-7.

Authors

Guillermo Velasco¹, Chris Armstrong, Nick Morrice, Sheelagh Frame, Philip Cohen

Affiliation

¹ Division of Signal Transduction Therapy, School of Life Sciences, University of Dundee, DD1 5EH, Dundee, UK.

PMID: 12220642
DOI: 10.1016/s0014-5793(02)03175-7

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Base Sequence
Catalytic Domain
Intracellular Signaling Peptides and Proteins
Molecular Sequence Data
Muscle, Smooth / metabolism*
Myosin-Light-Chain Phosphatase
Myosins / metabolism*
Phosphoprotein Phosphatases / genetics
Phosphoprotein Phosphatases / metabolism*
Phosphorylation
Protein Phosphatase 1
Protein Serine-Threonine Kinases / metabolism
Protein Subunits
Threonine / metabolism
rho-Associated Kinases

Substances

Intracellular Signaling Peptides and Proteins
Protein Subunits
Threonine
Protein Serine-Threonine Kinases
rho-Associated Kinases
Phosphoprotein Phosphatases
Protein Phosphatase 1
Myosin-Light-Chain Phosphatase
Myosins