p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C.
p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C.
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p65 片段与蛋白激酶 C 的 C2 区同源,与蛋白激酶 C 的细胞内受体结合。
DOI:
10.1021/bi00150a003
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发表时间:
1992
期刊:
影响因子:
2.9
通讯作者:
Smith,BL
中科院分区:
文献类型:
--
作者:
Mochly-Rosen,D;Miller,KG;Scheller,RH;Khaner,H;Lopez,J;Smith,BL
Revised Manuscript Received May 20, 1992 abstract: Receptors for activated protein kinase C (RACKs) have been isolated from the particulate cell fraction of heart and brain. We previously demonstrated that binding of protein kinase C (PKC) to RACKs requires PKC activators and is via a site on PKC that is distinct from the substrate binding site. Here, we examine the possibility that the C2 region in the regulatory domain of PKC is involved in binding of PKC to RACKs. The synaptic vesicle-specificp65 protein contains two regions homologous to the C2 region of PKC. We found that three p65 fragments, containing either one or two of these PKC C2 homologous regions, bound tohighly purified RACKs. Binding of the p65 fragments and PKC to RACKs was mutually exclusive; preincubation of RACKs with the p65 fragmentsinhibited PKC binding, and preincubation of RACKs with PKC inhibited binding of the p65 fragments. Preincubation of the p65 fragments with a peptide resembling the PKC binding site on RACKs also inhibited p65 binding to RACKs, suggesting that PKC and p65 bind to the same or nearby regions on RACKs. Since the only homologous region between PKC and the p65 fragments is the C2 region, these results suggest that the C2 region on PKC contains at least part of the RACK binding site.