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 Lettjournal_title
FEBS lettersauthors
Murányi A,Zhang R,Liu F,Hirano K,Ito M,Epstein HF,Hartshorne DJdoi
10.1016/s0014-5793(01)02283-9keywords:
subject
Has Abstractpub_date
2001-03-30 00:00:00pages
80-4issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02283-9journal_volume
493pub_type
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