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Phosphorylation of brush border myosin by brush border calmodulin‐dependent myosin heavy and light chain kinases
Author(s) -
Rieker James P.,
Collins Jimmy H.
Publication year - 1987
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(87)80301-0
Subject(s) - myosin light chain kinase , myosin , calmodulin , brush border , phosphorylation , immunoglobulin light chain , actin , kinase , biochemistry , biology , chemistry , biophysics , microbiology and biotechnology , enzyme , vesicle , membrane , antibody , immunology
Calmodulin‐dependent myosin light chain kinase isolated from chicken intestinal brush border phosphorylates brush border myosin at an apparently single serine identical to that phosphorylated by smooth muscle myosin light chain kinase. Phosphorylation to 1.8 mol phosphate/mol myosin activated the myosin actin‐activated ATPase about 10‐fold, to about 50 nmol/min per mg. Myosin phosphorylated on its light chains could then be further phosphorylated to a total of 3.2 mol phosphate per mol by brush border calmodulin‐dependent heavy chain kinase. Heavy chain phosphorylation did not alter the actin‐activated ATPase of either myosin prephosphorylated on its light chains or of unphosphorylated myosin.