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首页> 外文期刊>Biochemistry >Competitive Binding of Protein Kinase C alpha to Membranes and Rho GTPases
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Competitive Binding of Protein Kinase C alpha to Membranes and Rho GTPases

机译：蛋白激酶Cα与膜和Rho GTPases的竞争结合。

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Previously,we have shown that protein kinase Ca (PKCa) forms a direct high-affinity,isozyme-specific and membrane lipid-independent interaction with Rho GTPases [Slater,S.J.,Seiz,J.L.,Stagliano,B.A.,and Stubbs,C.D.(2001) Biochemistry 40,4437-4445].Since the cellular activation of PKCa involves an initial translocation from cytosolic to membrane compartments,the present study investigates the interdependence between the direct protein-protein interaction of PKCa with the Rho GTPase,Cdc42,and the protein-lipid interactions of PKCa with membranes.It was hypothesized that the interaction of PKCa with membrane-bound Cdc42 would contribute to the overall membrane-binding affinity of the kinase by providing an additional anchor.However,it was found that the incorporation of isoprenylated Cdc42 into membranes resulted in an apparent decrease in the membrane-binding affinity of PKCa,whereas the association of PKC beta I,PKC sigma,PKCepsilon,and PKC zeta was each unaffected.The presence of membrane-bound Cdc42 resulted in a rightward shift in both the PS-and Ca~(2+)-concentration response curves for PKCa membrane association and for the ensuing activation,whereas the maximal levels of binding and activation attained at saturating PS and Ca~(2+) concentrations were in each case unaffected.Overall,these findings suggest that PKCa undergoes a isozyme-specific interaction with membrane-bound Cdc42 to form a PKCa-Cdc42 complex,which possesses a membrane-binding affinity that is reduced relative to that of the individual components due to competition between Cdc42 and PS/Ca~(2+) for binding to PKCa.Consistent with this,it was found that the interaction of PKCa with membrane-bound Cdc42 was accompanied by the physical dissociation of the PKCa-Cdc42 complex from membranes.Thus,the study provides a novel mechanism by which the membrane association and activation of PKCa and Cdc42 may be regulated by competing protein-protein and protein-lipid interactions.
机译：以前，我们已经证明蛋白激酶Ca（PKCa）与Rho GTPases [Slater，SJ，Seiz，JL，Stagliano，BA，and Stubbs，CD（2001）形成直接的高亲和力，同工酶特异性和膜脂质非依赖性相互作用。 ）生物化学40,4437-4445]。由于PKCa的细胞活化涉及从胞质到膜区室的初始易位，因此本研究调查了PKCa与Rho GTPase，Cdc42和蛋白质之间直接的蛋白质相互作用。假设PKCa与膜结合的Cdc42的相互作用将通过提供额外的锚定而有助于激酶的整体膜结合亲和力。然而，发现异戊二烯基化的Cdc42的掺入进入膜中会导致PKCa的膜结合亲和力明显降低，而PKCβI，PKCσ，PKCepsilon和PKC zeta的关联均不受影响。烷结合的Cdc42导致PKCa膜缔合和随后的活化的PS和Ca〜（2+）浓度响应曲线向右移动，而饱和PS和Ca〜时达到的最大结合和活化水平（2+）浓度在每种情况下均不受影响。总体而言，这些发现表明PKCa与膜结合的Cdc42发生同工酶特异性相互作用，形成PKCa-Cdc42复合物，该复合物的膜结合亲和力相对于PKCa-Cdc42降低。 Cdc42与PS / Ca〜（2+）之间竞争与PKCa的结合导致了单个成分的变化。与此相一致，发现PKCa与膜结合的Cdc42的相互作用伴随着PKCa-的物理解离。因此，这项研究提供了一种新的机制，通过该机制，PKCa和Cdc42的膜缔合和激活可能受到竞争性蛋白质-蛋白质和蛋白质-脂质相互作用的调节。

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