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GTP/ggS‐Induced phosphorylation of myosin light chain kinase in smooth muscle
Author(s) -
Tang Da-Chun,
Kubota Yasutaka,
Kamm Kristine E.,
Stull James T.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80351-t
Subject(s) - myosin light chain kinase , phosphorylation , myosin , calmodulin , immunoglobulin light chain , chemistry , protein kinase a , microbiology and biotechnology , rho associated protein kinase , kinase , gtp' , biophysics , biochemistry , biology , enzyme , antibody , immunology
Phosphorylation of myosin light chain kinase by a Ca 2+ ‐dependent protein kinase increases the concentration of Ca 2+ /calmodulin required for half‐maximal activation. The Ca 2+ concentrations required for myosin light chain kinase phosphorylation in permeable smooth muscle are similar to those required for myosin light chain phosphorylation. Both GTPγS and carbachol increase the Ca 2+ sensitivity of myosin light chain kinase phosphorylation as well as light chain phosphorylation. It is proposed that a similar G‐protein mediated mechanism regulates the Ca 2+ ‐dependent phosphorylation of these two contractile proteins in smooth muscle.