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

20 sept. 2018eLife

DOI : 10.7554/elife.37262

Auteurs

Feng-Ching Tsai, Aurelie Bertin, Hugo Bousquet, John Manzi, Yosuke Senju, Meng-Chen Tsai, Laura Picas, Stephanie Miserey-Lenkei, Pekka Lappalainen, Emmanuel Lemichez, Evelyne Coudrier, Patricia Bassereau

Résumé

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 anti-parallelly, 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.

Equipes

Équipe

Membranes et fonctions cellulaires

PATRICIA BASSEREAU

Membres

PATRICIA BASSEREAU

Directeur de recherche CNRS

AURELIE BERTIN

Directeur de recherche CNRS

FENG CHING TSAI

Chargé de recherche CNRS