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pubmed:abstractText |
Type I inositol 1,4,5-trisphosphate receptors can be phosphorylated by cAMP-dependent protein kinase (PKA) and cGMP-dependent protein kinase (PKG). To define the site-specificity of these events we analyzed the phosphorylation of mutant receptors expressed in intact cells. These studies showed that S(1588) and S(1755), the serine residues within kinase consensus sequences, are equally sensitive to PKA, that phosphorylation events at these sites are independent of each other, and that PKG predominantly phosphorylates S(1588). These findings provide the basis for understanding the functional consequences of type I inositol 1,4,5-trisphosphate receptor phosphorylation.
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pubmed:affiliation |
Department of Pharmacology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210-2339, USA.
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