期刊
STRUCTURE
卷 22, 期 3, 页码 409-420出版社
CELL PRESS
DOI: 10.1016/j.str.2013.12.015
关键词
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资金
- Deutsche Forschungsgemeinschaft [SFB740, SFB958]
- Leibnitz Graduate School
- National Institutes of Health [GM063915]
- Swedish Medical Research Council
- Swedish Foundation for Strategic Research
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.
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