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

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

DOI:
10.1016/j.celrep.2021.109122
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发表时间:
2021-05-18
期刊:
影响因子:
8.8
通讯作者:
Bi E
Bi E
中科院分区:
生物学1区
文献类型:
--
作者:
Duan X;Chen X;Wang K;Chen L;Glomb O;Johnsson N;Feng L;Zhou XQ;Bi E

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细胞如何采用不同的形态来应对压力还不是很清楚。在这里,我们发现萌芽酵母Ecm25与极化的内吞部位结合,并通过不同的区域与极性调节因子CDC42和几个晚期内吞蛋白相互作用,包括肌动蛋白细丝结合基序。ECM25的缺失不会影响CDC42的活性,也不会在液相和笼状蛋白介导的内吞作用中造成任何严重的缺陷,但完全取消羟基脲诱导的细胞伸长。这种表型伴随着芽皮质中时空耦合的外吞饮作用的去极化,同时维持整个母芽的极性。这些数据表明,ECM25在极化信号和内吞机制之间提供了重要的联系,从而使胁迫条件下的适应性形态发生成为可能。细胞如何采用不同的形态来应对压力还不是很清楚。Duan et al.报道称,芽期酵母蛋白Ecm25通过将极性调节器CDC42连接到后期的内吞机械,在应激诱导的细胞伸长中发挥重要作用。
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. How cells adopt a different morphology to cope with stress is not well understood. Duan et al. report that the budding yeast protein Ecm25 plays an essential role in stress-induced cell elongation by linking the polarity regulator Cdc42 to the late-stage endocytic machinery.
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