Identification of the serine residue phosphorylated by protein kinase C in vertebrate nonmuscle myosin heavy chains.

Abstract:

:Two-dimensional mapping of the tryptic phosphopeptides generated following in vitro protein kinase C phosphorylation of the myosin heavy chain isolated from human platelets and chicken intestinal epithelial cells shows a single radioactive peptide. These peptides were found to comigrate, suggesting that they were identical, and amino acid sequence analysis of the human platelet tryptic peptide yielded the sequence -Glu-Val-Ser-Ser(PO4)-Leu-Lys-. Inspection of the amino acid sequence for the chicken intestinal epithelial cell myosin heavy chain (196 kDa) derived from cDNA cloning showed that this peptide was identical with a tryptic peptide present near the carboxyl terminal of the predicted alpha-helix of the myosin rod. Although other vertebrate nonmuscle myosin heavy chains retain neighboring amino acid sequences as well as the serine residue phosphorylated by protein kinase C, this residue is notably absent in all vertebrate smooth muscle myosin heavy chains (both 204 and 200 kDa) sequenced to date.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Conti MA,Sellers JR,Adelstein RS,Elzinga M

doi

10.1021/bi00218a012

subject

Has Abstract

pub_date

1991-01-29 00:00:00

pages

966-70

issue

4

eissn

0006-2960

issn

1520-4995

journal_volume

30

pub_type

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