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Protein kinase C phosphorylates both the light chains and the head portion of the heavy chains of brain myosin.

Abstract：

:Protein kinase C phosphorylated both the 19/21-kDa regulatory light chains and heavy chains of bovine brain myosin. The major phosphorylation sites of the light chains were on their threonyl residues, while those for myosin light chain kinase were on their seryl residues. Whereas several non-muscle regular myosins have been reported to be phosphorylated by different types of protein kinases at the non-helical small segments at the tail ends of the heavy chains, the phosphorylation sites for protein kinase C were localized on the head portion of the heavy chains of brain myosin. The possible role of phosphorylation of brain myosin by protein kinase C in the regulation of motility of neural cells is discussed.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Ikeda N,Yasuda S,Muguruma M,Matsumura S

doi

10.1016/0006-291x(90)92022-r

subject

Has Abstract

pub_date

1990-06-29 00:00:00

pages

1191-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)92022-R

journal_volume

169

pub_type

杂志文章

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