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首页> 外文期刊>Biochemistry >The C2 domain of the Ca2+-independent protein kinase C Apl II inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner
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The C2 domain of the Ca2+-independent protein kinase C Apl II inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner

机译：独立于Ca2 +的蛋白激酶C Apl II的C2结构域以磷脂酸敏感的方式抑制佛波酯与C1结构域的结合

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摘要

There are two protein kinase Cs (PKCs) in the Aplysia nervous system, PKC Apl I, which is homologous to the Ca2+-activated PKC family, and PKC Apl II, which is homologous to the Ca2+-independent PKCs epsilon and eta. Purified PKC Apl I requires much less phosphatidylserine for activation than does purified PKC Apl II, and this may explain why the neurotransmitter serotonin activates PKC Apl I but not PKC Apl II in the intact nervous system [Sossin, W. S., Fan, X., and Baseri, F. (1996) J. Neurosci. 16, 10-18]. PKC Apl II's requirement for high levels of phosphatidylserine may be mediated by its C2 domain, since removal of this domain allows PKC Apl II to be activated at lower concentrations of phosphatidylserine. To begin to understand how this inhibition is mediated, we generated fusion proteins containing the C1 and C2 domains from PKC Apl II and determined their lipid dependence for phorbol ester binding. Our results indicate that the presence of the C2 domain lowers the affinity of protein kinase C activators for the C1 domains and this inhibition can be removed by phosphatidylserine. Phosphatidic acid, however, is much more potent than phosphatidylserine in reducing C2 domain-mediated inhibition, suggesting that phosphatidic acid may be a required cofactor for the activation of PKC Apl II. [References: 66]
机译：在海nervous神经系统中有两个蛋白激酶Cs（PKCs），即与Ca2 +激活的PKC家族同源的PKC Apl I，和与不依赖Ca2 +的PKCsε和eta同源的PKC Apl II。纯化的PKC Apl I激活所需的磷脂酰丝氨酸比纯化的PKC Apl II少得多，这可以解释为什么神经递质5-羟色胺激活完整神经系统中的PKC Apl I而不激活PKC Apl II [Sossin，WS，Fan，X. and Baseri，F。（1996）J.Neurosci。 16、10-18]。 PKC Apl II对高水平磷脂酰丝氨酸的要求可能是由其C2结构域介导的，因为去除该结构域可使PKC Apl II在较低的磷脂酰丝氨酸浓度下被激活。为了开始理解这种抑制作用是如何介导的，我们从PKC Apl II中生成了包含C1和C2域的融合蛋白，并确定了它们对佛波酯结合的脂质依赖性。我们的结果表明，C2域的存在降低了蛋白激酶C激活剂对C1域的亲和力，这种抑制作用可以通过磷脂酰丝氨酸消除。然而，磷脂酸在减少C2结构域介导的抑制方面比磷脂酰丝氨酸更有效，这表明磷脂酸可能是激活PKC Apl II所需的辅因子。 [参考：66]

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