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Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
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2007 (English)In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 449, no 7164, 923-927 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2007. Vol. 449, no 7164, 923-927 p.
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
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URN: urn:nbn:se:umu:diva-42786DOI: 10.1038/nature06173PubMedID: 17914359OAI: oai:DiVA.org:umu-42786DiVA: diva2:410389
Available from: 2011-04-13 Created: 2011-04-13 Last updated: 2017-12-11Bibliographically approved

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