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Clathrin is important for normal actin dynamics and progression of Sla2p-containing patches during endocytosis in yeast

机译：网格蛋白对于酵母内吞过程中的正常肌动蛋白动力学和含Sla2p的斑块的进展很重要

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摘要

Clathrin is a major vesicle coat protein involved in receptor-mediated endocytosis. In yeast and higher eukaryotes, clathrin is recruited to the plasma membrane during the early stage of endocytosis along with clathrin-associated adaptors. As coated pits undergo maturation, a burst of actin polymerization accompanies and helps drive vesicle internalization. Here, we investigate the dynamics of clathrin relative to the early endocytic patch protein Sla2p. We find that clathrin is recruited to the cortex prior to Sla2p. In the absence of clathrin, normal numbers of Sla2p patches form, but many do not internalize or are dramatically delayed in completion of endocytosis. Patches that do internalize receive Sla1p late, which is followed by Abp1, which appears near the end of Sla2p lifetime. In addition, clathrin mutants develop actin comet tails, suggesting an important function in actin patch organization/dynamics. Similar to its mammalian counterparts, the light chain (LC) subunit of yeast clathrin interacts directly with the coiled-coil domain of Sla2p. A mutant of Sla2p that no longer interacts with LC (sla2 Delta 376-573) results in delayed progression of endocytic patches and aberrant actin dynamics. These data demonstrate an important role for clathrin in organization and progression of early endocytic patches to the late stages of endocytosis.
机译：网格蛋白是参与受体介导的内吞作用的主要囊泡外壳蛋白。在酵母和高等真核生物中，网格蛋白在胞吞作用的早期与网格蛋白相关的衔接子一起被募集到质膜上。当包膜的凹坑成熟时，伴随着肌动蛋白聚合的爆发并帮助推动囊泡的内在化。在这里，我们调查网格蛋白相对于早期内吞补丁蛋白Sla2p的动力学。我们发现网格蛋白在Sla2p之前被募集到皮质。在没有网格蛋白的情况下，会形成正常数量的Sla2p贴片，但许多没有内在化或内吞作用的完成明显延迟。进行内部化处理的补丁迟到了Sla1p，随后是Abp1，后者出现在Sla2p生命周期的尽头。此外，网格蛋白突变体产生肌动蛋白彗星尾巴，表明在肌动蛋白补丁组织/动力学中的重要功能。类似于其哺乳动物的对应物，酵母网格蛋白的轻链（LC）亚基直接与Sla2p的卷曲螺旋结构域相互作用。不再与LC相互作用的Sla2p突变体（sla2 Delta 376-573）会导致内吞斑块进展缓慢，肌动蛋白动力学异常。这些数据证明网格蛋白在早期内吞斑块的组织和进展到内吞作用后期中的重要作用。

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