Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling

Oliver Daumke (), Richard Lundmark, Yvonne Vallis, Sascha Martens, P. Jonathan G. Butler and Harvey T. McMahon ()
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Oliver Daumke: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK
Richard Lundmark: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK
Yvonne Vallis: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK
Sascha Martens: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK
P. Jonathan G. Butler: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK
Harvey T. McMahon: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK

Nature, 2007, vol. 449, issue 7164, 923-927

Abstract: Structural details of mouse EHD2 are provided along with in vitro and in vivo assays, showing how an EHD oligomer is formed and how perpendicular curvature stresses on a membrane surface can result in remodelling of membranes by EHD oligomeric rings. The functional implications of the EHD2 structure for understanding of membrane deformation are also discussed.

Date: 2007
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DOI: 10.1038/nature06173

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