Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity
Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity
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DOI：
10.1016/j.devcel.2006.05.008
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发表时间：
2006-07-01
影响因子：
11.8
通讯作者：
Drubin, David G.
中科院分区：
文献类型：
--
作者：
Sun, Yidi;Martin, Adam C.;Drubin, David G.
芽殖酵母内吞内化所必需的肌动蛋白聚合由四种成核促进因子 (NPF) 控制，每种因子在内吞位点表现出独特的动态行为。每个 NPF 如何发挥作用并被调节以将肌动蛋白组装限制到内吞内化的后期尚不清楚。 NPF生化活性的定量分析以及募集和调节机制的遗传分析定义了一条线性途径，其中内吞位点的蛋白质组成变化控制肌动蛋白的组装和功能。我们表明，酵母 WASP 在内吞位点启动肌动蛋白组装，并且这种组装和 WASP 招募酵母 WIP 样蛋白会招募具有 NPF 和运动活性的 I 型肌球蛋白。重要的是，I 型肌球蛋白运动和 NPF 活动是可分离的，并且两者都有助于内吞层向内运动，这可能代表膜内陷。这些结果揭示了肌动蛋白成核和肌球蛋白运动活动协同促进内吞内化的机制。
Actin polymerization essential for endocytic internalization in budding yeast is controlled by four nucleation promoting factors (NPFs) that each exhibits a unique dynamic behavior at endocytic sites. How each NPF functions and is regulated to restrict actin assembly to late stages of endocytic internalization is not known. Quantitative analysis of NPF biochemical activities, and genetic analysis of recruitment and regulatory mechanisms, defined a linear pathway in which protein composition changes at endocytic sites control actin assembly and function. We show that yeast WASP initiates actin assembly at endocytic sites and that this assembly and the recruitment of a yeast WIP-like protein by WASP recruit a type I myosin with both NPF and motor activities. Importantly, type I myosin motor and NPF activities are separable, and both contribute to endocytic coat inward movement, which likely represents membrane invagination. These results reveal a mechanism in which actin nucleation and myosin motor activity cooperate to promote endocytic internalization.