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

FEBS Letters

Soulsby, Matthew D¹  Alzayady, Kamil¹  Wojcikiewicz, Richard J.H¹  Xu, Qun¹ 

[1] Department of Pharmacology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210-2339, USA

关键词: Inositol 1;    4;    5-trisphosphate receptor;    Phosphorylation;    cAMP-dependent protein kinase;    cGMP-dependent protein kinase;    InsP3;    inositol 1;    4;    5-trisphosphate;    PKA;    cAMP-dependent protein kinase;    PKG;    cGMP-dependent protein kinase;    PGE1;    prostaglandin E1;    PKC;    protein kinase C;    PMA;    phorbol-12-myristate 13-acetate;    HEK;    human embryonic kidney;   

DOI  :  10.1016/S0014-5793(03)01487-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 S¹⁵⁸⁸ and S¹⁷⁵⁵, 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 S¹⁵⁸⁸. These findings provide the basis for understanding the functional consequences of type I inositol 1,4,5-trisphosphate receptor phosphorylation.

【 授权许可】

Unknown