The contribution of serine residues 1588 and 1755 to phosphorylation of the type I inositol 1,4,5-trisphosphate receptor by PKA and PKG

被引：28

作者：

Soulsby, MD ^{[1
]}

Alzayady, K ^{[1
]}

Xu, Q ^{[1
]}

Wojcikiewicz, JH ^{[1
]}

机构：

[1] SUNY Syracuse, Upstate Med Univ, Dept Pharmacol, Syracuse, NY 13210 USA

来源：

FEBS LETTERS | 2004年 / 557卷 / 1-3期

关键词：

inositol 1,4,5-trisphosphate receptor; phosphorylation; cAMP-dependent protein kinase; cGMP-dependent protein kinase;

D O I：

10.1016/S0014-5793(03)01487-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：181 / 184

页数：4

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