在支气管平滑肌细胞中 CPI-17 和 RACK1 蛋白之间的功能相互作用。
A functional interaction between CPI-17 and RACK1 proteins in bronchial smooth muscle cells.
机构信息
Department of Pharmacology, School of Pharmacy, Hoshi University, Tokyo, Japan.
出版信息
Biochem Biophys Res Commun. 2010 Oct 22;401(3):487-90. doi: 10.1016/j.bbrc.2010.09.086. Epub 2010 Sep 25.
Abstract
CPI-17 is a phosphorylation-dependent inhibitor of smooth muscle myosin light chain. Using yeast two-hybrid system, we have identified the receptor for activated C kinase 1 (RACK1) as a novel interaction partner of CPI-17. The direct interaction and co-localization of CPI-17 with RACK1 were confirmed by immunoprecipitation and confocal microscopy analysis, respectively. An in vitro assay system using recombinant/purified proteins revealed that the PKC-mediated phosphorylation of CPI-17 was augmented in the presence of RACK1. These results suggest that RACK1 may play a role in PKC/CPI-17 signaling pathway.
摘要
CPI-17 是一种磷酸化依赖性的平滑肌肌球蛋白轻链抑制剂。我们利用酵母双杂交系统鉴定出蛋白激酶 C 激活受体 1（RACK1）是 CPI-17 的一个新的相互作用伙伴。免疫沉淀和共聚焦显微镜分析分别证实了 CPI-17 与 RACK1 的直接相互作用和共定位。利用重组/纯化蛋白的体外测定系统表明，在 RACK1 存在的情况下，PKC 介导的 CPI-17 磷酸化增强。这些结果表明，RACK1 可能在 PKC/CPI-17 信号通路中发挥作用。
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