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首页> 外文期刊>The Journal of biological chemistry >Cyclase-associated Protein (CAP) Acts Directly on F-actin to Accelerate Cofilin-mediated Actin Severing across the Range of Physiological pH
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Cyclase-associated Protein (CAP) Acts Directly on F-actin to Accelerate Cofilin-mediated Actin Severing across the Range of Physiological pH

机译：环酶相关蛋白（帽）直接用F-Actin作用，以加速辛脲介导的肌动蛋白在生理pH范围内切断

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Fast actin depolymerization is necessary for cells to rapidly reorganize actin filament networks. Utilizing a Listeria fluorescent actin comet tail assay to monitor actin disassembly rates, we observed that although a mixture of actin disassembly factors (cofilin, coronin, and actin-interacting protein 1 is sufficient to disassemble actin comet tails in the presence of physiological G-actin concentrations this mixture was insufficient to disassemble actin comet tails in the presence of physiological F-actin concentrations. Using biochemical complementation, we purified cyclase-associated protein (CAP) from thymus extracts as a factor that protects against the inhibition of excess F-actin. CAP has been shown to participate in actin dynamics but has been thought to act by liberating cofilin from ADP·G-actin monomers to restore cofilin activity. However, we found that CAP augments cofilin-mediated disassembly by accelerating the rate of cofilin-mediated severing. We also demonstrated that CAP acts directly on F-actin and severs actin filaments at acidic, but not neutral, pH. At the neutral pH characteristic of cytosol in most mammalian cells, we demonstrated that neither CAP nor cofilin are capable of severing actin filaments. However, the combination of CAP and cofilin rapidly severed actin at all pH values across the physiological range. Therefore, our results reveal a new function for CAP in accelerating cofilin-mediated actin filament severing and provide a mechanism through which cells can maintain high actin turnover rates without having to alkalinize cytosol, which would affect many biochemical reactions beyond actin depolymerization.
机译：快速肌动蛋白解聚对于细胞迅速重新组织actin灯丝网络是必需的。利用Histeria荧光肌动蛋白彗星尾部测定来监测肌动蛋白拆卸速率，我们观察到actin拆卸因子（Cofilin，Coronin和Actin-Interaction蛋白1的混合物足以在生理G- actin的存在下拆卸肌动蛋白彗星尾部浓度该混合物在生理F型肌动蛋白浓度存在下不充分地拆卸肌动蛋白彗星尾部。使用生化互补，我们将来自胸腺提取物的环酶相关蛋白（帽）纯化为保护过量F-actin的抑制的因素。已显示帽子参与肌动蛋白动态，但已被通过从ADP·G-Actin单体中解放Cofilin来恢复辛菌素活性的行为。然而，我们发现Cap通过加速辛苷介导的切断速率来增强辛硅介导的拆卸。我们还证明了CAP直接在F-Actin和Sepers actin长丝在酸性，而不是中性的pH值。在NE大多数哺乳动物细胞中胞质醇的utral pH值特征，我们证明既不盖也不能够切断肌动蛋白长丝。然而，帽和甲状腺素的组合在整个生理范围的所有pH值中快速切断肌动蛋白。因此，我们的结果揭示了加速Cofilin介导的肌动蛋白细丝切割的新功能，并提供了细胞可以保持高肌动蛋白周转率而不具有碱化细胞溶溶胶的机制，这会影响肌动蛋白解聚的许多生化反应。

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