Supramolecular organization of the human N-BAR domain in shaping the sarcolemma membrane
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...
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| Veröffentlicht in: | Journal of structural biology 2016-06, Vol.194 (3), p.375-382 |
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| container_title | Journal of structural biology |
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| creator | Daum, Bertram Auerswald, Andrea Gruber, Tobias Hause, Gerd Balbach, Jochen Kühlbrandt, Werner Meister, Annette |
| description | 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. |
| doi_str_mv | 10.1016/j.jsb.2016.03.017 |
| format | Article |
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| subjects | Adaptor Proteins, Signal Transducing - chemistry Cryoelectron Microscopy CryoEM CryoET Humans Membrane curvature Membrane lipid composition Membrane Proteins - metabolism Membranes - ultrastructure Muscle, Skeletal - chemistry Muscle, Skeletal - ultrastructure N-BAR domain Nuclear Proteins - chemistry Protein Domains - physiology Protein Multimerization Sarcolemma Sarcolemma - ultrastructure Subtomogram averaging Tomography Tumor Suppressor Proteins - chemistry |
| title | Supramolecular organization of the human N-BAR domain in shaping the sarcolemma membrane |
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