دورية أكاديمية
A human septin octamer complex sensitive to membrane curvature drives membrane deformation with a specific mesh-like organization
العنوان: | A human septin octamer complex sensitive to membrane curvature drives membrane deformation with a specific mesh-like organization |
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المؤلفون: | Nakazawa, Koyomi, Kumar, Gaurav, Chauvin, Brieuc, Cicco, Aurélie Di, Pellegrino, Luca, Trichet, Michaël, Hajj, Bassam, Cabral, João, Sain, Anirban, Mangenot, Stéphanie, Bertin, Aurélie |
المساهمون: | Laboratoire Physico-Chimie Curie Institut Curie (PCC), Institut Curie Paris -Institut de Chimie - CNRS Chimie (INC-CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Indian Institute of Science Bangalore (IISc Bangalore), Department of Chemical Engineering London, Imperial College London, Microscopie Electronique IBPS (IBPS-ME), Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU), Indian Institute of Technology Bombay (IIT Bombay), Matière et Systèmes Complexes (MSC), Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Fondation pour la Recherche MédicaleAAP Emergence (Sorbonne Université), ANR-13-JSV8-0002,SEPTIME,Assemblage et ultrastructure des septines, de la molécule à la cellule(2013), ANR-20-CE11-0014,SeptScort,Interaction spatiale et fonctionnelle entre septines et Escrt pendant la cytocinèse: une approche multi-échelle(2020) |
المصدر: | ISSN: 0021-9533. |
بيانات النشر: | HAL CCSD Company of Biologists |
سنة النشر: | 2023 |
مصطلحات موضوعية: | [SDV]Life Sciences [q-bio] |
الوصف: | International audience ; Septins are cytoskeletal proteins interacting with the inner plasma membrane and other cytoskeletal partners. Being key in membrane remodeling processes, they often localize at specific micrometric curvatures. To analyze the behavior of human septins at the membrane and decouple their role from other partners, we used a combination of bottom-up in vitro methods. We assayed their ultrastructural organization, their curvature sensitivity, as well as their role in membrane reshaping. On membranes, human septins organize into a two-layered mesh of orthogonal filaments, instead of generating parallel sheets of filaments observed for budding yeast septins. This peculiar mesh organization is sensitive to micrometric curvature and drives membrane reshaping as well. The observed membrane deformations together with the filamentous organization are recapitulated in a coarse-grained computed simulation to understand their mechanisms. Our results highlight the specific organization and behavior of animal septins at the membrane as opposed to those of fungal proteins. |
نوع الوثيقة: | article in journal/newspaper |
اللغة: | English |
العلاقة: | hal-04236725; https://cnrs.hal.science/hal-04236725Test; https://cnrs.hal.science/hal-04236725/documentTest; https://cnrs.hal.science/hal-04236725/file/Nakazawa_ms_jcs.pdfTest |
DOI: | 10.1242/jcs.260813 |
الإتاحة: | https://doi.org/10.1242/jcs.260813Test https://cnrs.hal.science/hal-04236725Test https://cnrs.hal.science/hal-04236725/documentTest https://cnrs.hal.science/hal-04236725/file/Nakazawa_ms_jcs.pdfTest |
حقوق: | http://creativecommons.org/licenses/byTest/ ; info:eu-repo/semantics/OpenAccess |
رقم الانضمام: | edsbas.1AC4DD12 |
قاعدة البيانات: | BASE |
DOI: | 10.1242/jcs.260813 |
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