| First Author | Shah C | Year | 2014 |
| Journal | Structure | Volume | 22 |
| Issue | 3 | Pages | 409-420 |
| PubMed ID | 24508342 | Mgi Jnum | J:222668 |
| Mgi Id | MGI:5645194 | Doi | 10.1016/j.str.2013.12.015 |
| Citation | Shah C, et al. (2014) Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2. Structure 22(3):409-20 |
| abstractText | The dynamin-related Eps15-homology domain-containing protein 2 (EHD2) is a membrane-remodeling ATPase that regulates the dynamics of caveolae. Here, we established an electron paramagnetic resonance (EPR) approach to characterize structural features of membrane-bound EHD2. We show that residues at the tip of the helical domain can insert into the membrane and may create membrane curvature by a wedging mechanism. Using EPR and X-ray crystallography, we found that the N terminus is folded into a hydrophobic pocket of the GTPase domain in solution and can be released into the membrane. Cryoelectron microscopy demonstrated that the N terminus is not essential for oligomerization of EHD2 into a membrane-anchored scaffold. Instead, we found a function of the N terminus in regulating targeting and stable association of EHD2 to caveolae. Our data uncover an unexpected, membrane-induced regulatory switch in EHD2 and demonstrate the versatility of EPR to study structure and function of dynamin superfamily proteins. |
