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| Item Type: | Article |
|---|---|
| Title: | EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization |
| Creators Name: | Moren, B. and Shah, C. and Howes, M.T. and Schieber, N.L. and McMahon, H.T. and Parton, R.G. and Daumke, O. and Lundmark, R. |
| Abstract: | EHD2 belongs to the Eps15 homology (EH) domain containing protein family of dynamin-related ATPases involved in membrane remodeling in the endosomal system. EHD2 dimers oligomerize into rings on highly curved membranes resulting in stimulation of the intrinsic ATPase activity. Here, we report that EHD2 is specifically and stably associated with caveolae at the plasma membrane and not involved in clathrin-mediated endocytosis or endosomal recycling, as previously suggested. EHD2 interacts with pacsin2 and cavin1 and ordered membrane assembly of EHD2 is dependent on cavin1 and caveolae integrity. While the EH domain of EHD2 is dispensable for targeting, we identified a loop in the nucleotide binding domain that together with ATP-binding is required for caveola localization. EHD2 was not essential for the formation or shaping of caveolae but high levels of EHD2 caused distortion and loss of endogenous caveolae. Assembly of EHD2 stabilized and constrained caveolae to the plasma membrane to control turnover, and depletion of EHD2 resulted in endocytic and more dynamic and short-lived caveolae. Thus, following the identification of caveolin and cavins, EHD2 constitutes a third structural component of caveolae involved in controlling the stability and turnover of this organelle. |
| Keywords: | EHD2, Caveolae, Membrane Remodeling, Dynamin-Like, Animals, Mice |
| Source: | Molecular Biology of the Cell |
| ISSN: | 1059-1524 |
| Publisher: | American Society for Cell Biology |
| Volume: | 23 |
| Number: | 7 |
| Page Range: | 1316-1329 |
| Date: | 9 February 2012 |
| Official Publication: | https://doi.org/10.1091/mbc.E11-09-0787 |
| PubMed: | View item in PubMed |
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