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Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase

AuthorsBenguria, Alberto; Hernández-Perera, Octavio; Martínez-Pastor, María Teresa; Sacks, David B.; Villalobo, Antonio
Issue DateSep-1994
CitationEuropean Journal of Biochemistry 224(3): 909-916 (1994)
AbstractAn epidermal-growth-factor(EGF)-receptor preparation isolated by calmodulin-affinity chromatography from rat liver plasma membranes is able to phosphorylate calmodulin. Calmodulin phosphorylation was enhanced 3–8-fold by EGF, was dependent on the presence of a polycation or basic protein and was inhibited by micromolar concentrations of Ca2+. Phosphate incorporation into calmodulin occurs predominantly on tyrosine residues. Partial proteolysis of phosphocalmodulin by thrombin identifies Tyr99, located in the third calcium-binding domain of calmodulin, as the phosphorylated residue. Stoichiometric measurements show a 32P/calmodulin molar ratio of approximately 1 when optimal phosphorylation conditions are used.
Description8 pages, 9 figures.-- Now known as FEBS Journal: Open Access content older than 1 year.
Publisher version (URL)http://dx.doi.org/10.1111/j.1432-1033.1994.00909.x
Appears in Collections:(IIBM) Artículos
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