Phosphorylation of vertebrate smooth muscle and nonmuscle myosin heavy chains in vitro and in intact cells.

Content Provider	Semantic Scholar
Author	Kawamoto, Sachiyo Conti, Mary Anne Adelstein, Robert S.
Copyright Year	1991
Abstract	In this article we summarize our recent experiments studying the phosphorylation of vertebrate myosin heavy chains by protein kinase C and casein kinase II. Protein kinase C phosphorylates vertebrate non-muscle myosin heavy chains both in vitro and in intact cells. A single serine residue near the end of the helical portion of the myosin rod is the only site phosphorylated in a variety of vertebrate nonmuscle myosin heavy chains. There does not appear to be a site for protein kinase C phosphorylation in vertebrate smooth muscle myosin heavy chains. Casein kinase II phosphorylates a single serine residue located near the carboxyl terminus of the 204 x 10(3) Mr smooth muscle myosin heavy chain in vitro as well as in cultured smooth muscle cells. It does not phosphorylate the 200 x 10(3) Mr smooth muscle myosin heavy chain. However, the site is present in vertebrate nonmuscle myosin heavy chains. The 204 x 10(3) Mr myosin heavy chain of embryonic chicken gizzard smooth muscle is exceptional in not containing a site for casein kinase II phosphorylation.
Starting Page	49
Ending Page	54
Page Count	6
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://jcs.biologists.org/content/joces/1991/Supplement_14/49.full.pdf
PubMed reference number	1885659v1
Volume Number	14
Journal	Journal of cell science. Supplement
Language	English
Access Restriction	Open
Subject Keyword	Carboxyl Group Casein Kinase II Caseins Gizzard Immunoglobulin kappa-Chains Myosin Heavy Chains Protein Kinase C Protein Kinases SLC3A2 gene Smooth muscle (tissue) eIF-2 Kinase
Content Type	Text
Resource Type	Article