TY - JOUR TI - Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner AU - Tsai, Feng-Ching AU - Bertin, Aurelie AU - Bousquet, Hugo AU - Manzi, John AU - Senju, Yosuke AU - Tsai, Meng-Chen AU - Picas, Laura AU - Miserey-Lenkei, Stephanie AU - Lappalainen, Pekka AU - Lemichez, Emmanuel AU - Coudrier, Evelyne AU - Bassereau, Patricia A2 - Akhmanova, Anna A2 - Fritzsche, Marco VL - 7 PY - 2018 DA - 2018/09/20 SP - e37262 C1 - eLife 2018;7:e37262 DO - 10.7554/eLife.37262 UR - https://doi.org/10.7554/eLife.37262 AB - 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. KW - ezrin KW - membrane curvature KW - I-BAR domain proteins KW - ezrin-membrane interaction KW - cellular protrusions KW - phosphorylation JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -