Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner
Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner
Abstract One challenge in current 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 or with positive or negative curvatures. Using in vitro and cell biology approaches, we assess mechanisms of ezrin’s enrichment on curved membranes. We evidence that 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 ezrin interactions, allows binding to actin filaments, and promotes ezrin binding to positively curved membranes. While neither ezrinTD nor ezrinWT senses negative membrane curvature alone, we demonstrate that interacting with curvature sensors I-BAR-domain proteins facilitates ezrin enrichment in negatively curved membrane protrusions. Overall, our work reveals new mechanisms, specific conformation or binding to a curvature sensor partner, for targeting curvature insensitive proteins to curved membranes.
Bousquet Hugo、Tsai Meng-Chen、Lemichez Emmanuel、Coudrier Evelyne、Bassereau Patricia、Tsai Feng-Ching、Miserey-Lenkei St¨|phanie、Bertin Aur¨|lie、Lappalainen Pekka、Picas Laura、Senju Yosuke、Manzi John
Institut Curie, PSL Research University and C.N.R.S. UMR 144Mediterranean Center of Molecular Medecine (C3M), Inserm U1065, University of C?te d?ˉAzurMediterranean Center of Molecular Medecine (C3M), Inserm U1065, University of C?te d?ˉAzurInstitut Curie, PSL Research University and C.N.R.S. UMR 144Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168||Sorbonne Universit¨|s, UPMC University Paris 06Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168||Sorbonne Universit¨|s, UPMC University Paris 06Institut Curie, PSL Research University and C.N.R.S. UMR 144Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168||Sorbonne Universit¨|s, UPMC University Paris 06Program in Cell and Molecular Biology, Institute of BiotechnologyInstitut de Recherche en Infectiologie de Montpellier (IRIM) and C.N.R.S. UMR 9004Program in Cell and Molecular Biology, Institute of BiotechnologyLaboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168||Sorbonne Universit¨|s, UPMC University Paris 06
细胞生物学生物物理学分子生物学
Bousquet Hugo,Tsai Meng-Chen,Lemichez Emmanuel,Coudrier Evelyne,Bassereau Patricia,Tsai Feng-Ching,Miserey-Lenkei St¨|phanie,Bertin Aur¨|lie,Lappalainen Pekka,Picas Laura,Senju Yosuke,Manzi John.Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner[EB/OL].(2025-03-28)[2025-05-17].https://www.biorxiv.org/content/10.1101/297895.点此复制
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