The contribution of serine residues 1588 and 1755 to phosphorylation of the type I inositol 1,4,5-trisphosphate receptor by PKA and PKG.
The contribution of serine residues 1588 and 1755 to phosphorylation of the type I inositol 1,4,5-trisphosphate receptor by PKA and PKG.
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丝氨酸残基 1588 和 1755 对 PKA 和 PKG 磷酸化 I 型肌醇 1,4,5-三磷酸受体的贡献。
DOI：
10.1016/s0014-5793(03)01487-x
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发表时间：
2004
期刊：
影响因子：
3.5
通讯作者：
Wojcikiewicz,RichardJH
中科院分区：
文献类型：
--
作者：
Soulsby,MatthewD;Alzayady,Kamil;Xu,Qun;Wojcikiewicz,RichardJH
I型肌醇1，4，5-三磷酸受体可被cAMP依赖性蛋白激酶（PKA）和cGMP依赖性蛋白激酶（PKG）磷酸化。为了确定这些事件的位点特异性，我们分析了完整细胞中表达的突变受体的磷酸化。这些研究表明，激酶共有序列中的丝氨酸残基S1588和S1755对PKA同样敏感，这些位点的磷酸化事件彼此独立，PKG主要磷酸化S1588。这些发现为理解I型肌醇1，4，5-三磷酸受体磷酸化的功能后果提供了基础。
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 S1588and 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.