| First Author | Wang Q | Year | 2008 |
| Journal | Structure | Volume | 16 |
| Issue | 10 | Pages | 1574-87 |
| PubMed ID | 18940612 | Mgi Jnum | J:247406 |
| Mgi Id | MGI:5926309 | Doi | 10.1016/j.str.2008.07.016 |
| Citation | Wang Q, et al. (2008) Structure and plasticity of Endophilin and Sorting Nexin 9. Structure 16(10):1574-87 |
| abstractText | Endophilin and Sorting Nexin 9 (Snx9) play key roles in endocytosis by membrane curvature sensing and remodeling via their Bin/Amphiphysin/Rvs (BAR) domains. BAR and the related F-BAR domains form dimeric, crescent-shaped units that occur N- or C-terminally to other lipid-binding, adaptor, or catalytic modules. In crystal structures, the PX-BAR unit of Snx9 (Snx9(PX-BAR)) adopts an overall compact, moderately curved conformation. SAXS-based solution studies revealed an alternative, more curved state of Snx9(PX-BAR) in which the PX domains are flexibly connected to the BAR domains, providing a model for how Snx9 exhibits lipid-dependent curvature preferences. In contrast, Endophilin appears to be rigid in solution, and the SH3 domains are located at the distal tips of a BAR domain dimer with fixed curvature. We also observed tip-to-tip interactions between the BAR domains in a trigonal crystal form of Snx9(PX-BAR) reminiscent of functionally important interactions described for F-BAR domains. |
