Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains
- 1 November 1993
- journal article
- research article
- Published by Springer Nature in Molecular and Cellular Biochemistry
- Vol. 127-128 (1) , 219-227
- https://doi.org/10.1007/bf01076773
Abstract
In this article we review the various amino acids present in vertebrate nonmuscle and smooth muscle myosin that can undergo phosphorylation. The sites for phosphorylation in the 20 kD myosin light chain include serine-19 and threonine-18 which are substrates for myosin light chain kinase and serine-1 and/or-2 and threonine-9 which are substrates for protein kinase C. The sites in vertebrate smooth muscle and nonmuscle myosin heavy chains that can be phosphorylated by protein kinase C and casein kinase II are also summarized. Original data indicating that treatment of human T-lymphocytes (Jurkat cell line) with phorbol 12-myristate 13-acetate results in phosphorylation of both the 20 kD myosin light chain as well as the 200 kD myosin heavy chain is presented. We identified the amino acids phosphorylated in the human T-lymphocytes myosin light chains as serine-1 or serine-2 and in the myosin heavy chains as serine-1917 by 1-dimensional isoelectric focusing of tryptic phosphopeptides. Untreated T-lymphocytes contain phosphate in the serine-19 residue of teh myosin light chain and in a residue tentatively identified as serine-1944 in the myosin heavy chain.Keywords
This publication has 55 references indexed in Scilit:
- Catalytic fragment of protein kinase C exhibits altered substrate specificity toward smooth muscle myosin light chainFEBS Letters, 1991
- Protein kinase C phosphorylates both the light chains and the head portion of the heavy chains of brain myosinBiochemical and Biophysical Research Communications, 1990
- Myosin heavy chain isoform diversity in smooth muscle is produced by differential RNA processingJournal of Molecular Biology, 1989
- Filamentous smooth muscle myosin is regulated by phosphorylation.The Journal of cell biology, 1989
- Effects of modulators of myosin light-chain kinase activity in single smooth muscle cellsNature, 1989
- Phosphorylation site sequence of smooth muscle myosin light chain (Mr = 20 000)FEBS Letters, 1984
- Regulation of the actin-myosin interaction in vertebrate smooth muscle: Activation via a myosin light-chain kinase and the effect of tropomyosinJournal of Molecular Biology, 1977
- The effect of phosphorylation of gizzard myosin on actin activationBiochemical and Biophysical Research Communications, 1976
- Myosin-linked calcium regulation in vertebrate smooth muscleJournal of Molecular Biology, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970