title: Supramolecular organization of the human N-BAR domain in shaping the sarcolemma membrane.
abstract: The 30kDa N-BAR domain of the human Bin1 protein is essential for the generation of skeletal muscle T-tubules. By electron cryo-microscopy and electron cryo-tomography with a direct electron detector, we found that Bin1-N-BAR domains assemble into scaffolds of low long-range order that form flexible membrane tubules. The diameter of the tubules closely matches the curved shape of the N-BAR domain, which depends on the composition of the target membrane. These insights are fundamental to our understanding of T-tubule formation and function in human skeletal muscle.
authors.affiliation: Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany.
authors.forename: Bertram
authors.initials: B
authors.lastname: Daum
authors.affiliation: Mitteldeutsches Zentrum für Struktur und Dynamik der Proteine, ZIK HALOmem, Martin Luther University Halle-Wittenberg, 06120 Halle, Germany.
authors.forename: Andrea
authors.initials: A
authors.lastname: Auerswald
authors.affiliation: Biophysics, Institute of Physics, Betty-Heimann-Str. 7, Martin Luther University Halle-Wittenberg, 06120 Halle, Germany.
authors.forename: Tobias
authors.initials: T
authors.lastname: Gruber
authors.affiliation: Microscopy Unit, Biocenter, Weinbergweg 22, Martin Luther University Halle-Wittenberg, 06120 Halle, Germany.
authors.forename: Gerd
authors.initials: G
authors.lastname: Hause
authors.affiliation: Mitteldeutsches Zentrum für Struktur und Dynamik der Proteine, ZIK HALOmem, Martin Luther University Halle-Wittenberg, 06120 Halle, Germany; Biophysics, Institute of Physics, Betty-Heimann-Str. 7, Martin Luther University Halle-Wittenberg, 06120 Halle, Germany.
authors.forename: Jochen
authors.initials: J
authors.lastname: Balbach
authors.affiliation: Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany. Electronic address: werner.kuehlbrandt@biophys.mpg.de.
authors.forename: Werner
authors.initials: W
authors.lastname: Kühlbrandt
authors.affiliation: Mitteldeutsches Zentrum für Struktur und Dynamik der Proteine, ZIK HALOmem, Martin Luther University Halle-Wittenberg, 06120 Halle, Germany. Electronic address: annette.meister@chemie.uni-halle.de.
authors.forename: Annette
authors.initials: A
authors.lastname: Meister
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry*; D020285:Cryoelectron Microscopy; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008566:Membranes / Q000648:ultrastructure; D018482:Muscle, Skeletal / Q000737:chemistry / Q000648:ultrastructure; D009687:Nuclear Proteins / Q000737:chemistry*; D000072417:Protein Domains / Q000502:physiology*; D055503:Protein Multimerization; D012508:Sarcolemma / Q000648:ultrastructure*; D014054:Tomography; D025521:Tumor Suppressor Proteins / Q000737:chemistry*
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C101410:BIN1 protein, human; D008565:Membrane Proteins; D009687:Nuclear Proteins; D025521:Tumor Suppressor Proteins
keywords: CryoEM; CryoET; Membrane curvature; Membrane lipid composition; N-BAR domain; Sarcolemma; Subtomogram averaging