Membrane binding controls ordered self-assembly of animal septins
| Autor: | Ralf P. Richter, Aurélie Bertin, Gerard Castro-Linares, Gijsje H. Koenderink, Francois, Agata Szuba, Manos Mavrakis, Fouzia Bano |
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| Přispěvatelé: | Laboratory of Physico-chemistry of Life, CNRS, Institut Curie, F-75005 Paris, affiliation inconnue, FOM Institute for Atomic and Molecular Physics (AMOLF), University of Leeds, Kavli Institute of Nanosciences [Delft] (KI-NANO), Delft University of Technology (TU Delft), Institut FRESNEL (FRESNEL), Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Aix Marseille Université (AMU), MOSAIC (MOSAIC), Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Aix Marseille Université (AMU), 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), ANR-17-CE13-0014,SEPTIMORF,Rôle des septines dans la morphogenèse des cellules animales(2017), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS), School of Biomedical Sciences, Faculty of Biological Sciences |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Protein Conformation
Structural Biology and Molecular Biophysics [SDV]Life Sciences [q-bio] Mutant Lipid Bilayers [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] Microscopy Atomic Force Septin plasma membrane Animals Genetically Modified 0302 clinical medicine [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB] Drosophila Proteins Biology (General) Cytoskeleton 0303 health sciences D. melanogaster Chemistry General Neuroscience Microfilament Proteins cytoskeleton General Medicine [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics Drosophila melanogaster Membrane cortex Transmission electron microscopy Medicine biological phenomena cell phenomena and immunity Research Article Human Protein Binding QH301-705.5 Science Stacking [SDV.BC]Life Sciences [q-bio]/Cellular Biology macromolecular substances General Biochemistry Genetics and Molecular Biology Membrane Lipids Structure-Activity Relationship 03 medical and health sciences Microscopy Electron Transmission Cell cortex Animals Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology cell surface mechanics 030304 developmental biology General Immunology and Microbiology Cell Membrane Cryoelectron Microscopy Molecular biophysics fungi [SDV.BDD.MOR]Life Sciences [q-bio]/Development Biology/Morphogenesis Cell Biology Structural biology Quartz Crystal Microbalance Techniques Biophysics Self-assembly Protein Multimerization Septins 030217 neurology & neurosurgery |
| Zdroj: | eLife eLife, eLife Sciences Publication, 2021, 10, pp.e63349. ⟨10.7554/eLife.63349⟩ eLife, Vol 10 (2021) eLife, 2021, 10, pp.e63349. ⟨10.7554/eLife.63349⟩ eLife, 10 |
| ISSN: | 2050-084X |
| Popis: | Septins are conserved cytoskeletal proteins that regulate cell cortex mechanics. The mechanisms of their interactions with the plasma membrane remain poorly understood. Here we show by cell-free reconstitution that membrane binding requires electrostatic interactions of septins with anionic lipids and promotes the ordered self-assembly of fly septins into filamentous meshworks. Transmission electron microscopy reveals that both fly and mammalian septins form arrays of single and paired filaments. Atomic force microscopy and quartz crystal microbalance demonstrate that the fly filaments form mechanically rigid, 12 to 18 nm thick, double layers of septins. By contrast, C-terminally truncated septin mutants form 4 nm thin monolayers, indicating that stacking requires the C-terminal coiled coils on DSep2 and Pnut subunits. Our work shows that membrane binding is required for fly septins to form ordered arrays of single and paired filaments and provides new insights into the mechanisms by which septins may regulate cell surface mechanics. |
| Databáze: | OpenAIRE |
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