The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3‘:5‘ cAMP-dependent protein kinase.

Conti, M.A.; Adelstein, R.S.

doi:10.1016/s0021-9258(19)69586-4

Cited by 390

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3‘:5‘ cAMP-dependent protein kinase.

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Conti, M.A., Adelstein, R.S.·1981·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(19)69586-4

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Smooth muscle myosin light chain kinase, a calmodulin-dependent enzyme, binds 1 mol of calmodulin/mol of kinase in the presence of calcium (Adelstein, R. S., and Klee, C. B. (1981) J. Biol. Chem. 256, in press. This enzyme is a substrate for cAMP-dependent protein kinase whether or not calmodulin is bound. When calmodulin is not bound to myosin kinase, protein kinase incorporates phosphate into two sites in myosin kinase. Under these circumstances, phosphorylation markedly lowers the rate of myosin kinase activity. The decrease in myosin kinase activity is due to a 10-20-fold increase in the amount of calmodulin necessary for 50% activation of kinase activity. The effect of phosphorylation on the activity of myosin kinase can be reversed by dephosphorylation using a purified phosphatase (Pato, M. D., and Adelstein, R. S. (1980) J. Biol. Chem. 255, 6535-6538) isolated from smooth muscle. When calmodulin is bound to myosin kinase, phosphate is incorporated into a single site with no effect on myosin kinase activity. The presence of at least two sites that can be phosphorylated in myosin kinase was confirmed by tryptic digestion of denatured myosin kinase.

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Authors: Conti, M. A., & Adelstein, R. S.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1981-04
Volume: 256
Issue: 7
Pages: 3178-3181
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(19)69586-4
OpenAlex: W1596707465
Cited by: 390
References: 19
FWCI: 11.85
Type: journal article
Language: en
Open access: hybrid

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This page: CoChat. (2026). Citation check: The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3‘:5‘ cAMP-dependent protein kinase. https://app.cochat.ai/papers/10.1016/s0021-9258(19)69586-4
The paper: Conti, M. A., & Adelstein, R. S. (1981). The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3‘:5‘ cAMP-dependent protein kinase. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)69586-4

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The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3‘:5‘ cAMP-dependent protein kinase.

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