Correlative AFM and fluorescence imaging demonstrate nanoscale membrane remodeling and ring-like and tubular structure formation by septins
Autor: | Stéphanie Mangenot, Cyntia Taveneau, Hussein Nasrallah, Brieuc Chauvin, Daniel Lévy, Cédric Godefroy, Luca Costa, Patrice Dosset, Pierre-Emmanuel Milhiet, Aurélie Bertin, Anthony Vial, Kien Xuan Ngo, Hervé Isambert |
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Přispěvatelé: | Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire Physico-Chimie Curie [Institut Curie] (PCC), Institut Curie [Paris]-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Kanazawa University (KU) |
Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
Fluorescence-lifetime imaging microscopy
Structure formation Saccharomyces cerevisiae Proteins Cell division Saccharomyces cerevisiae macromolecular substances Ring (chemistry) Septin fluorescence microscopy 03 medical and health sciences reshaping 0302 clinical medicine General Materials Science [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Lipid bilayer Nanoscopic scale membrane Cytoskeleton 030304 developmental biology 0303 health sciences Chemistry Cell Membrane Optical Imaging fungi Atomic Force Microscopy Membrane curvature Biophysics biological phenomena cell phenomena and immunity 030217 neurology & neurosurgery Septins |
Zdroj: | Nanoscale Nanoscale, Royal Society of Chemistry, In press, ⟨10.1039/D1NR01978C⟩ |
ISSN: | 2040-3364 2040-3372 |
DOI: | 10.1039/D1NR01978C⟩ |
Popis: | International audience; Septins are ubiquitous cytoskeletal filaments that interact with the inner plasma membrane and are essential for cell division in eukaryotes. In cellular contexts, septins are often localized at micrometric Gaussian curvatures, where they assemble onto ring-like structures. The behavior of budding yeast septins depends on their specific interaction with inositol phospholipids, enriched at the inner leaflet of the plasma membrane. Septin filaments are built from the non-polar self-assembly of short rods into filaments. However, the molecular mechanisms regulating the interplay with the inner plasma membrane and the resulting interaction with specific curvatures are not fully understood. In this report, we have imaged dynamical molecular assemblies of budding yeast septins on PIP2-containing supported lipid bilayers using a combination of high-speed AFM and correlative AFM-fluorescence microscopy. Our results clearly demonstrate that septins are able to bind to flat supported lipid bilayers and thereafter induce the remodeling of membranes. Short septin rods (octamers subunits) can indeed destabilize supported lipid bilayers and reshape the membrane to form 3D structures such as rings and tubes, demonstrating that long filaments are not necessary for septin-induced membrane buckling. |
Databáze: | OpenAIRE |
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