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The contribution of serine residues 1588 and 1755 to phosphorylation of the type I inositol 1,4,5‐trisphosphate receptor by PKA and PKG
Author(s) -
Soulsby Matthew D,
Alzayady Kamil,
Xu Qun,
Wojcikiewicz Richard J.H
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01487-x
Subject(s) - phosphorylation , inositol , protein kinase a , chemistry , serine , receptor , protein phosphorylation , inositol trisphosphate , cgmp dependent protein kinase , inositol phosphate , microbiology and biotechnology , biochemistry , biology , mitogen activated protein kinase kinase
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.