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Essential Role of the Endocytic Site-Associated Protein Ecm25 in Stress-Induced Cell Shape Change
69 Pages Posted: 24 Apr 2020 Publication Status: Published
More...Abstract
How cells adopt a different morphology to cope with stress is not well understood. Here, we show that Ecm25, a previously uncharacterized protein in budding yeast, associates with polarized endocytic sites, and interacts with the polarity regulator Cdc42 and several late-stage endocytic proteins via distinct domains or motifs, including an unexpected actin filament-binding site. Deletion of ECM25 does not affect Cdc42 activity or cause any strong defects in fluid-phase and clathrin-mediated endocytosis. However, deletion of ECM25 completely abolishes cell elongation – a form of sustained polarized cell growth induced by chemical or genetic perturbations. This phenotype is accompanied by depolarization of the spatiotemporally coupled exo-endocytosis in the bud cortex while maintaining the overall mother-bud polarity. Collectively, these data suggest that Ecm25 provides an essential link between the polarization signal and the endocytic machinery to enable adaptive morphogenesis under stressed conditions.
Keywords: Cell shape, endocytosis, exocytosis, Cdc42, actin patches, hydroxyurea, yeast
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