Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner

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http://hdl.handle.net/10138/299079

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Tsai , F-C , Bertin , A , Bousquet , H , Manzi , J , Senju , Y , Tsai , M-C , Picas , L , Miserey-Lenkei , S , Lappalainen , P , Lemichez , E , Coudrier , E & Bassereau , P 2018 , ' Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner ' , eLife , vol. 7 , 37262 . https://doi.org/10.7554/eLife.37262

Title: Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner
Author: Tsai, Feng-Ching; Bertin, Aurelie; Bousquet, Hugo; Manzi, John; Senju, Yosuke; Tsai, Meng-Chen; Picas, Laura; Miserey-Lenkei, Stephanie; Lappalainen, Pekka; Lemichez, Emmanuel; Coudrier, Evelyne; Bassereau, Patricia
Contributor: University of Helsinki, Institute of Biotechnology
University of Helsinki, Doctoral Programme in Integrative Life Science
Date: 2018-09-20
Language: eng
Number of pages: 27
Belongs to series: eLife
ISSN: 2050-084X
URI: http://hdl.handle.net/10138/299079
Abstract: One challenge in cell biology is to decipher the biophysical mechanisms governing protein enrichment on curved membranes and the resulting membrane deformation. The ERM protein ezrin is abundant and associated with cellular membranes that are flat, positively or negatively curved. Using in vitro and cell biology approaches, we assess mechanisms of ezrin's enrichment on curved membranes. We evidence that wild-type ezrin (ezrinWT) and its phosphomimetic mutant T567D (ezrinTD) do not deform membranes but self-assemble antiparallelly, zipping adjacent membranes. EzrinTD's specific conformation reduces intermolecular interactions, allows binding to actin filaments, which reduces membrane tethering, and promotes ezrin binding to positively-curved membranes. While neither ezrinTD nor ezrinWT senses negative curvature alone, we demonstrate that interacting with curvature-sensing I-BAR-domain proteins facilitates ezrin enrichment in negatively-curved membrane protrusions. Overall, our work demonstrates that ezrin can tether membranes, or be targeted to curved membranes, depending on conformations and interactions with actin and curvature-sensing binding partners.
Subject: GIANT UNILAMELLAR VESICLES
F-ACTIN BINDING
EPITHELIAL-CELLS
ERM PROTEINS
PHYSIOLOGICAL CONDITIONS
QUANTITATIVE-ANALYSIS
CYTOSKELETAL LINKER
NATIVE MEMBRANES
APICAL MEMBRANE
PARIETAL-CELLS
1182 Biochemistry, cell and molecular biology
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