A human septin octamer complex sensitive to membrane curvature drives membrane deformation with a specific mesh-like organization.


Journal

Journal of cell science
ISSN: 1477-9137
Titre abrégé: J Cell Sci
Pays: England
ID NLM: 0052457

Informations de publication

Date de publication:
01 06 2023
Historique:
received: 16 11 2022
accepted: 04 05 2023
medline: 13 6 2023
pubmed: 12 6 2023
entrez: 12 6 2023
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 37305997
pii: 316658
doi: 10.1242/jcs.260813
pmc: PMC10281262
pii:
doi:

Substances chimiques

Septins EC 3.6.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© 2023. Published by The Company of Biologists Ltd.

Déclaration de conflit d'intérêts

Competing interests The authors declare no competing or financial interests.

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Auteurs

Koyomi Nakazawa (K)

Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, Sorbonne Université, CNRS UMR168, 75005, Paris, France.

Gaurav Kumar (G)

Molecular Biophysics Unit, Indian Institute of Science Bangalore, Bangalore, Karnataka 560012, India.

Brieuc Chauvin (B)

Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, Sorbonne Université, CNRS UMR168, 75005, Paris, France.

Aurélie Di Cicco (A)

Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, Sorbonne Université, CNRS UMR168, 75005, Paris, France.

Luca Pellegrino (L)

Department of Chemical Engineering, Imperial College London, London SW7 2AZ, UK.

Michael Trichet (M)

Sorbonne Université, CNRS, Institut de Biologie Paris-Seine (IBPS), Service de microscopie électronique (IBPS-SME), F-75005, Paris, France.

Bassam Hajj (B)

Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, Sorbonne Université, CNRS UMR168, 75005, Paris, France.

João Cabral (J)

Department of Chemical Engineering, Imperial College London, London SW7 2AZ, UK.

Anirban Sain (A)

Department of Physics, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India.

Stéphanie Mangenot (S)

Laboratoire Matière et Systèmes Complexes (MSC), Université Paris Cité, CNRS UMR 7057, 75006 Paris, France.

Aurélie Bertin (A)

Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, Sorbonne Université, CNRS UMR168, 75005, Paris, France.

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