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首页> 外文期刊>Biochemistry >Interactionof Protein Kinase C Isozymes with Rho GTPases
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Interactionof Protein Kinase C Isozymes with Rho GTPases

机译：蛋白激酶C同工酶与Rho GTPases的相互作用

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Evidence is provided for direct protein—protein interactions between protein kinase C (PKC) cL, /31, j311, y, 6, E, and ~ and members of the Rho family of small GTPases. Previous investigations, based on the immunoprecipitation approach, have provided evidence consistent with a direct interaction, but this remained to be proven. In the study presented here, an in vitro assay, consisting only of purified proteins and the requisite PKC activators and cofactors, was used to determine the effects of Rho GTPases on the activities of the different PKC isoforms. It was found that the activity of PKCct was potently enhanced by RhoA and Cdc42 and to a lesser extent by Raci, whereas the effects on the activities of PKC/31, -/311, -y, -6, -E, and -~ were much reduced. These results indicate a direct interaction between PKCcL and each of the Rho GTPases. However, the Rho GTPase concentration dependencies for the potentiating effects on PKCt activity differed for each Rho GTPase and were in the following order:RhoA> Cdc42> Raci. PKCct was activated in a phorbol ester- and Ca2±~dependent manner. This was reflected by a substantial decrease in the phorbol ester concentration requirements for activity in the presence of Ca2±, which for each Rho GTPase was induced within a low nanomolar phorbol ester concentration range. The activity of PKCct also was found to be dependent on the nature of the GTP- or GDP-bound state of the Rho GTPases, suggesting that the interaction may be regulated by conformational changes in both PKCcL and Rho GTPases. Such an interaction could result in significant cross-talk between the distinct pathways regulated by these two signaling elements.
机译：提供了蛋白质激酶C（PKC）cL，/ 31，j311，y，6，E和〜与小GTPase的Rho家族成员之间直接蛋白质相互作用的证据。先前基于免疫沉淀方法的研究提供了与直接相互作用一致的证据，但这仍有待证明。在此处介绍的研究中，仅由纯化的蛋白质以及必需的PKC激活剂和辅因子组成的体外测定法用于确定Rho GTPases对不同PKC同工型活性的影响。发现RhoA和Cdc42有效地增强了PKCct的活性，而Raci对PKCct的活性增强的程度较小，而对PKC / 31，-/ 311，-y，-6，-E和-〜的活性的影响较大。大大减少了。这些结果表明PKCcL和每个Rho GTPases之间直接相互作用。然而，每种Rho GTP酶对PKCt活性增强作用的Rho GTP酶浓度依赖性不同，其顺序如下：RhoA> Cdc42> Raci。 PKCct以佛波酯和Ca2 +依赖性方式被激活。这反映为在存在Ca2±的情况下，佛波酯浓度对活性的要求大大降低，对于每种Rho GTP酶，其在低纳摩尔佛波醇酯浓度范围内均被诱导。还发现PKCct的活性取决于Rho GTPases的GTP或GDP结合状态的性质，这表明相互作用可能受PKCcL和Rho GTPases构象变化的调节。这种相互作用可能导致在这两个信号元件调节的不同途径之间产生明显的串扰。

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