TYROSINE PHOSPHORYLATION OF PROTEIN-KINASE C-DELTA IN RESPONSE TO THE ACTIVATION OF THE HIGH-AFFINITY RECEPTOR FOR IMMUNOGLOBULIN-E MODIFIES ITS SUBSTRATE RECOGNITION
TYROSINE PHOSPHORYLATION OF PROTEIN-KINASE C-DELTA IN RESPONSE TO THE ACTIVATION OF THE HIGH-AFFINITY RECEPTOR FOR IMMUNOGLOBULIN-E MODIFIES ITS SUBSTRATE RECOGNITION
复制标题
DOI：
10.1073/pnas.92.20.9112
复制
发表时间：
1995-09-26
影响因子：
11.1
通讯作者：
RIVERA, J
中科院分区：
文献类型：
--
作者：
HALEEMSMITH, H;CHANG, EY;RIVERA, J
蛋白激酶C的δ型异构体在免疫球蛋白E高亲和受体的抗原激活下在酪氨酸上磷酸化，而蛋白激酶C- δ与该受体结合并磷酸化，受体的免疫沉淀显示很少（如果有的话）酪氨酸磷酸化的蛋白激酶C- δ与受体相关。免疫沉淀酪氨酸磷酸化蛋白激酶c - δ的体外激酶试验表明，修饰后的酶对作为底物的受体γ链肽的活性降低，但对组蛋白或髓鞘碱性蛋白肽的活性没有降低。我们提出了一个模型，其中蛋白激酶c - δ的酪氨酸磷酸化调节了对给定底物的激酶特异性，这可能代表了体内蛋白激酶活性在响应外部刺激时被调节的一般机制。
The delta isoform of protein kinase C is phosphorylated on tyrosine in response to antigen activation of the high-affinity receptor for immunoglobulin E, While protein kinase C-delta associates with and phosphorylates this receptor, immunoprecipitation of the receptor revealed that little, if any, tyrosine-phosphorylated protein kinase C-delta is receptor associated, rn vitro kinase assays with immunoprecipitated tyrosine-phosphorylated protein kinase C-delta showed that the modified enzyme had diminished activity toward the receptor gamma-chain peptide as a substrate but not toward histones or myelin basic protein peptide. We propose a model in which the tyrosine phosphorylation of protein kinase C-delta regulates the kinase specificity toward a given substrate, This may represent a general mechanism by which in vivo protein kinase activities are regulated in response to external stimuli.