| First Author | Daumke O | Year | 2007 |
| Journal | Nature | Volume | 449 |
| Issue | 7164 | Pages | 923-7 |
| PubMed ID | 17914359 | Mgi Jnum | J:126923 |
| Mgi Id | MGI:3762310 | Doi | 10.1038/nature06173 |
| Citation | Daumke O, et al. (2007) Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling. Nature 449(7164):923-927 |
| abstractText | The ability to actively remodel membranes in response to nucleotide hydrolysis has largely been attributed to GTPases of the dynamin superfamily, and these have been extensively studied. Eps15 homology (EH)-domain-containing proteins (EHDs/RME-1/pincher) comprise a less-well-characterized class of highly conserved eukaryotic ATPases implicated in clathrin-independent endocytosis, and recycling from endosomes. Here we show that EHDs share many common features with the dynamin superfamily, such as a low affinity for nucleotides, the ability to tubulate liposomes in vitro, oligomerization around lipid tubules in ring-like structures and stimulated nucleotide hydrolysis in response to lipid binding. We present the structure of EHD2, bound to a non-hydrolysable ATP analogue, and provide evidence consistent with a role for EHDs in nucleotide-dependent membrane remodelling in vivo. The nucleotide-binding domain is involved in dimerization, which creates a highly curved membrane-binding region in the dimer. Oligomerization of dimers occurs on another interface of the nucleotide-binding domain, and this allows us to model the EHD oligomer. We discuss the functional implications of the EHD2 structure for understanding membrane deformation. |
