内吞位点相关蛋白 Ecm25 在应激诱导的细胞伸长中的重要作用。

Essential role of the endocytic site-associated protein Ecm25 in stress-induced cell elongation.

机构信息

Department of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6058, USA; Animal Nutrition Institute, Sichuan Agricultural University, Chengdu, 611130 Sichuan, China; Chongqing Institute of Green and Intelligent Technology, Chinese Academy of Sciences, Chongqing 400714, China.

Department of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6058, USA.

出版信息

Cell Rep. 2021 May 18;35(7):109122. doi: 10.1016/j.celrep.2021.109122.

DOI:10.1016/j.celrep.2021.109122

PMID:34010635

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8202958/

Abstract

How cells adopt a different morphology to cope with stress is not well understood. Here, we show that budding yeast Ecm25 associates with polarized endocytic sites and interacts with the polarity regulator Cdc42 and several late-stage endocytic proteins via distinct regions, including an actin filament-binding motif. Deletion of ECM25 does not affect Cdc42 activity or cause any strong defects in fluid-phase and clathrin-mediated endocytosis but completely abolishes hydroxyurea-induced cell elongation. This phenotype is accompanied by depolarization of the spatiotemporally coupled exo-endocytosis in the bud cortex while maintaining the overall mother-bud polarity. These data suggest that Ecm25 provides an essential link between the polarization signal and the endocytic machinery to enable adaptive morphogenesis under stress conditions.

摘要

细胞如何通过改变形态来应对压力还不是很清楚。在这里，我们发现出芽酵母 Ecm25 与极化的内吞位点结合，并通过不同的区域与极性调节剂 Cdc42 和几个晚期内吞蛋白相互作用，包括一个肌动蛋白丝结合基序。ECM25 的缺失不影响 Cdc42 的活性，也不会导致液相等和网格蛋白介导的内吞作用出现明显缺陷，但完全消除了羟基脲诱导的细胞伸长。这种表型伴随着芽皮质中时空偶联的外-内吞作用的去极化，同时保持整体母-芽极性。这些数据表明，Ecm25 在极化信号和内吞机制之间提供了一个必要的联系，使细胞能够在应激条件下进行适应性形态发生。