Phosphorylation of smooth muscle myosin by type II Ca2+/calmodulin-dependent protein kinase
- 1 September 1990
- journal article
- research article
- Published by Springer Nature in Molecular and Cellular Biochemistry
- Vol. 97 (1) , 87-98
- https://doi.org/10.1007/bf00231704
Abstract
Brain type II Ca2+/calmodulin-dependent protein kinase was found to phoshorylate smooth muscle myosin, incorporating maximally ∼ 2 mol of phosphoryl per mol of myosin, exclusively on the 20,000 dalton light chain subunit. After maximal phosphorylation of myosin or the isolated 20,000 dalton light chain subunit by myosin light chain kinase, the addition of type II Ca2+/calmodulin-dependent protein kinase led to no further incorporation indicating the two kinases phosphorylated a common site. This conclusion was supported by two dimensional mapping of tryptic digests of myosin phosphorylated by the two kinases. By phosphoamino acid analysis the phosphorylated residue was identified as a serine. The phosphorylation by type II Ca 2+/calmodulin-dependent protein kinase of myosin resulted in enhancement of its actin-activated Mg2+-ATPase activity. Taken together, these data strongly support the conclusion that type II Ca2+/calmodulin-dependent protein kinase phosphorylates the same amino acid residue on the 20,000 dalton light chain subunit of smooth muscle myosin as is phosphorylated by myosin light chain kinase and suggest an alternative mechanism for the regulation of actin-myosin interaction.This publication has 58 references indexed in Scilit:
- Calcium dependence of myosin light chain phosphorylation in smooth muscle cells.Journal of Biological Chemistry, 1988
- Regulation of embryonic smooth muscle myosin by protein kinase C.Journal of Biological Chemistry, 1988
- Phosphorylation of two sites on smooth muscle myosin. Effects on contraction of glycerinated vascular smooth muscle.Journal of Biological Chemistry, 1988
- Phosphorylation of the 20,000-dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation.Journal of Biological Chemistry, 1987
- Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20,000-dalton light chain of smooth muscle myosin.Journal of Biological Chemistry, 1986
- Relationship between cytoplasmic free calcium and myosin light chain phosphorylation in intact plateletsBiochemical Journal, 1985
- Distinct forebrain and cerebellar isozymes of type II Ca2+/calmodulin-dependent protein kinase associate differently with the postsynaptic density fraction.Journal of Biological Chemistry, 1985
- Selective purification of the 20,000-Da light chains of smooth muscle myosinAnalytical Biochemistry, 1983
- Phosphorylation of skeletal muscle myosin light chain kinase by the catalytic subunit of cAMP‐dependent protein kinaseFEBS Letters, 1982
- PHOSPHORYLATION OF SMOOTH-MUSCLE MYOSIN LIGHT-CHAINS BY CAMP-DEPENDENT PROTEIN-KINASE1980