Structural insights into membrane interaction and caveolar targeting of 
dynamin-like EHD2

Shah, C.; Hegde, B. G.; Morén, B.; Behrmann, E.; Mielke, T.; Moenke, G.; Spahn, C. M. T.; Lundmark, R.; Daumke, O.; Langen, R.

doi:10.1016/j.str.2013.12.015

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Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2

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http://www.ncbi.nlm.nih.gov/pubmed/24508342
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Shah, C., Hegde, B. G., Morén, B., Behrmann, E., Mielke, T., Moenke, G., et al. (2014). Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2. Structure, 22(3), 409-20. doi:10.1016/j.str.2013.12.015.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-6372-5

Abstract

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.