Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity.

Abstract:

:Myotonic dystrophy protein kinase (DMPK) and Rho-kinase are related. An important function of Rho-kinase is to phosphorylate the myosin-binding subunit of myosin phosphatase (MYPT1) and inhibit phosphatase activity. Experiments were carried out to determine if DMPK could function similarly. MYPT1 was phosphorylated by DMPK. The phosphorylation site(s) was in the C-terminal part of the molecule. DMPK was not inhibited by the Rho-kinase inhibitors, Y-27632 and HA-1077. Several approaches were taken to determine that a major site of phosphorylation was T654. Phosphorylation at T654 inhibited phosphatase activity. Thus both DMPK and Rho-kinase may regulate myosin II phosphorylation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Murányi A,Zhang R,Liu F,Hirano K,Ito M,Epstein HF,Hartshorne DJ

doi

10.1016/s0014-5793(01)02283-9

keywords:

subject

Has Abstract

pub_date

2001-03-30 00:00:00

pages

80-4

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02283-9

journal_volume

493

pub_type

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