Supramolecular organization of the human N-BAR domain in shaping the sarcolemma membrane
Daum, B; Auerswald, A; Gruber, T; et al.Hause, G; Balbach, J; Kühlbrandt, W; Meister, A
Date: 22 March 2016
Journal
Journal of Structural Biology
Publisher
Elsevier
Publisher DOI
Abstract
The 30 kDa 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 30 kDa 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.
Physics and Astronomy
Faculty of Environment, Science and Economy
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