Tea4p links microtubule plus ends with the formin For3p in the establishment of cell polarity
Tea4p links microtubule plus ends with the formin For3p in the establishment of cell polarity
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DOI：
10.1016/j.devcel.2005.02.008
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发表时间：
2005-04-01
影响因子：
11.8
通讯作者：
Chang, F
中科院分区：
文献类型：
--
作者：
Martin, SG;McDonald, WH;Chang, F
微管调节基于肌动蛋白的过程，如细胞迁移和胞质分裂，但分子机制尚不清楚。在裂解酵母中，微管+末端部分通过将kelch重复蛋白tea1p运输到细胞末端来调节细胞极性。在这里，我们识别了tea4p，一种直接与teal p结合的SH3结构域蛋白。与teal p一样，tea4p定位于生长中的微管+末端和细胞末端的皮质部位，它是建立双极生长所必需的。Tea4P直接结合并募集3P的福尔明，3P使肌动蛋白电缆组装成核。在“新末端起飞”(Neto)过程中，形成包括teal p、tea4p和for3p的蛋白质复合体是建立细胞极性和在新细胞末端定位肌动蛋白组装的必要条件和充分条件。我们的结果提示了微管和末端如何调节肌动蛋白组装的空间分布的分子机制。
Microtubules regulate actin-based processes such as cell migration and cytokinesis, but molecular mechanisms are not understood. In the fission yeast Schizosaccharomyces pombe, microtubule plus ends regulate cell polarity in part by transporting the kelch repeat protein tea1p to cell ends. Here, we identify tea4p, a SH3 domain protein that binds directly to teal p. Like teal p, tea4p localizes to growing microtubule plus ends and to cortical sites at cell ends, and it is necessary for the establishment of bipolar growth. Tea4p binds directly to and recruits the formin for3p, which nucleates actin cable assembly. During "new end take off" (NETO), formation of a protein complex that includes teal p, tea4p, and for3p is necessary and sufficient for the establishment of cell polarity and localized actin assembly at new cell ends. Our results suggest a molecular mechanism for how microtubule plus ends regulate the spatial distribution of actin assembly.