| dc.contributor.author | Daum, B | |
| dc.contributor.author | Auerswald, A | |
| dc.contributor.author | Gruber, T | |
| dc.contributor.author | Hause, G | |
| dc.contributor.author | Balbach, J | |
| dc.contributor.author | Kühlbrandt, W | |
| dc.contributor.author | Meister, A | |
| dc.date.accessioned | 2018-02-13T16:03:29Z | |
| dc.date.issued | 2016-03-22 | |
| dc.description.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 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. | en_GB |
| dc.description.sponsorship | This work was supported by grants from the Deutsche Forschungsgemeinschaft (GRK 1026, SFB610) (A.A., T.G., J.B.), the BMBF ZIK program (A.M., J.B.), the European Regional Development Fund of the European Commission (A.M., T.G.: EFRE 1241 12 0001), and the state Sachsen-Anhalt (A.M., T.G., J.B.). | en_GB |
| dc.identifier.citation | Vol. 194 (3), pp. 375 - 382 | en_GB |
| dc.identifier.doi | 10.1016/j.jsb.2016.03.017 | |
| dc.identifier.uri | http://hdl.handle.net/10871/31461 | |
| dc.language.iso | en | en_GB |
| dc.publisher | Elsevier | en_GB |
| dc.rights | © 2016 The Authors. Published by Elsevier Inc. Open access. Under a Creative Commons license: https://creativecommons.org/licenses/by-nc-nd/4.0/ | en_GB |
| dc.subject | N-BAR domain | en_GB |
| dc.subject | Membrane lipid composition | en_GB |
| dc.subject | Membrane curvature | en_GB |
| dc.subject | Sarcolemma | en_GB |
| dc.subject | CryoEM | en_GB |
| dc.subject | CryoET | en_GB |
| dc.subject | Subtomogram averaging | en_GB |
| dc.title | Supramolecular organization of the human N-BAR domain in shaping the sarcolemma membrane | en_GB |
| dc.type | Article | en_GB |
| dc.date.available | 2018-02-13T16:03:29Z | |
| dc.identifier.issn | 1047-8477 | |
| dc.description | This is the final version of the article. Available from Elsevier via the DOI in this record. | en_GB |
| dc.identifier.journal | Journal of Structural Biology | en_GB |
