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Phosphorylation of calmodulin by plasma-membrane-associated protein kinase(s)

AuthorsBenguria, Alberto; Soriano, Montserrat; Joyal, John L.; Sacks, David B.; Villalobo, Antonio
Issue Date1995
CitationEuropean Journal of Biochemistry 234(1): 50-58 (1995)
AbstractPlasma-membrane-associated protein kinase(s) from normal rat liver phosphorylates exogenous bovine brain calmodulin in the absence of Ca2+ and in the presence of histone or poly(L-lysine). Maximum levels of calmodulin phosphorylation are obtained at a poly(L-lysine)/calmodulin molar ratio of 0.4. Phosphoamino acid analysis revealed that calmodulin is phosphorylated on serine, threonine and tyrosine residues. Endogenous plasma-membrane-associated calmodulin was also phosphorylated by plasma-membrane-associated protein kinase(s) in the absence of added cationic protein or polypeptide. The identity of endogenous phosphocalmodulin was confirmed by immunoprecipitation with a specific anti-calmodulin monoclonal antibody. Ehrlich ascites tumor cell plasma membranes do not contain endogenous calmodulin. However, membrane-associated protein kinase(s) from these tumor cells phosphorylates bovine brain calmodulin in the presence of poly(L-lysine). These data demonstrate that phosphocalmodulin is present in liver plasma membranes and suggest that this post-translational modification could have a physiological role in this location.
DescriptionNow known as FEBS Journal: Open Access content older than 1 year.
Publisher version (URL)http://dx.doi.org/10.1111/j.1432-1033.1995.050_c.x
Identifiersdoi: 10.1111/j.1432-1033.1995.050_c.x
issn: 0014-2956
e-issn: 1432-1033
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