Biochemical and Biophysical Research Communications
Volume 216, Issue 1, 2 November 1995, Pages 90-102
Regular ArticlePhosphorylation of Myosin-I from Rat Liver by Protein Kinase C Reduces Calmodulin Binding
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Cited by (14)
Calmodulin-binding proteins in the model organism Dictyostelium: A complete & critical review
2008, Cellular SignallingCalmodulin interacts with the third intracellular loop of the serotonin 5-hydroxytryptamine<inf>1A</inf> receptor at two distinct sites: Putative role in receptor phosphorylation by protein kinase C
2004, Journal of Biological ChemistryCitation Excerpt :Significant evidence suggests that phosphorylation of CaM-binding domains and the binding of CaM to a target protein can be mutually exclusive and in some cases antagonistic. Phosphorylation of target proteins by PKC has been shown to reduce binding of CaM to myosin 1 (50), the plasma membrane Ca2+ pump (51, 52), and calcium transport-like (CaT1) protein (53). Likewise, binding of CaM to neural tissue-enriched acidic protein (NAP-22) inhibits phosphorylation by PKC (54).
Regulation of the enzymatic and motor activities of myosin I
2000, Biochimica et Biophysica Acta - Molecular Cell ResearchRegulation of class I and class II myosins by heavy chain phosphorylation
1996, Journal of Biological Chemistry
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