Related Experiment Video
Updated: Nov 5, 2025

Measuring Cell-Edge Protrusion Dynamics during Spreading using Live-Cell Microscopy
Published on: November 1, 2021
Essential role of the endocytic site-associated protein Ecm25 in stress-induced cell elongation
Xudong Duan1, Xi Chen2, Kangji Wang2
1Department 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.
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.
More Related Videos
Related Concept Videos
Role of Microtubules in Cell Wall Deposition
Cell Motility through Blebbing
Blebbing Through the Matrix
In multicellular...
Mechanism of Lamellipodia Formation
Cytoskeletal Coordination in Cell Migration
Stringent Response in E. coli
Actin Polymerization and Cell Motility
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....

