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SLAC a complex between Sla1 and Las17 regulates actin polymerization during clathrin-mediated endocytosis

机译:SLACSla1和Las17之间的复合物在网格蛋白介导的胞吞过程中调节肌动蛋白的聚合

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摘要

During clathrin-mediated endocytosis, branched actin polymerization nucleated by the Arp2/3 complex provides force needed to drive vesicle internalization. Las17 (yeast WASp) is the strongest activator of the Arp2/3 complex in yeast cells; it is not autoinhibited and arrives to endocytic sites 20 s before actin polymerization begins. It is unclear how Las17 is kept inactive for 20 s at endocytic sites, thus restricting actin polymerization to late stages of endocytosis. In this paper, we demonstrate that Las17 is part of a large and biochemically stable complex with Sla1, a clathrin adaptor that inhibits Las17 activity. The interaction is direct, multivalent, and strong, and was mapped to novel Las17 polyproline motifs that are simultaneously class I and class II. In vitro pyrene-actin polymerization assays established that Sla1 inhibition of Las17 activity depends on the class I/II Las17 polyproline motifs and is based on competition between Sla1 and monomeric actin for binding to Las17. Furthermore, live-cell imaging showed the interaction with Sla1 is important for normal Las17 recruitment to endocytic sites, inhibition during the initial 20 s, and efficient endocytosis. These results advance our understanding of the regulation of actin polymerization in endocytosis.
机译:在网格蛋白介导的内吞作用过程中,Arp2 / 3复合物成核的支链肌动蛋白聚合反应提供了驱动囊泡内化所需的力。 Las17(酵母WASp)是酵母细胞中Arp2 / 3复合物最强的激活剂。它不是自动抑制的,在肌动蛋白聚合反应开始前20秒钟到达内吞位点。尚不清楚Las17如何在内吞位点保持失活20 s,从而将肌动蛋白聚合限制在内吞作用的后期。在本文中,我们证明Las17是与Sla1结合的大型生物化学稳定复合物的一部分,Sla1是一种抑制Las17活性的网格蛋白衔接子。相互作用是直接的,多价的和强的,并被映射到同时属于I类和II类的新型Las17多脯氨酸基序。体外pyr-肌动蛋白聚合试验确定,Sla1对Las17活性的抑制取决于I / II类Las17多脯氨酸基序,并且基于Sla1和单体肌动蛋白之间与Las17结合的竞争。此外,活细胞成像显示与Sla1的相互作用对于正常Las17募集到内吞位点,在最初20 s内抑制和有效的内吞作用很重要。这些结果提高了我们对内吞作用中肌动蛋白聚合调控的认识。

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