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Cryo-electron tomography structure of membrane-bound EHD4 complex
Structural highlights
FunctionEHD4_MOUSE ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport.[1] Publication Abstract from PubMedEps15-homology domain containing proteins (EHDs) are eukaryotic, dynamin-related ATPases involved in cellular membrane trafficking. They oligomerize on membranes into filaments that induce membrane tubulation. While EHD crystal structures in open and closed conformations were previously reported, little structural information is available for the membrane-bound oligomeric form. Consequently, mechanistic insights into the membrane remodeling mechanism have remained sparse. Here, by using cryo-electron tomography and subtomogram averaging, we determined structures of nucleotide-bound EHD4 filaments on membrane tubes of various diameters at an average resolution of 7.6 A. Assembly of EHD4 is mediated via interfaces in the G-domain and the helical domain. The oligomerized EHD4 structure resembles the closed conformation, where the tips of the helical domains protrude into the membrane. The variation in filament geometry and tube radius suggests a spontaneous filament curvature of approximately 1/70 nm(-1). Combining the available structural and functional data, we suggest a model for EHD-mediated membrane remodeling. Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments.,Melo AA, Sprink T, Noel JK, Vazquez-Sarandeses E, van Hoorn C, Mohd S, Loerke J, Spahn CMT, Daumke O Nat Commun. 2022 Dec 10;13(1):7641. doi: 10.1038/s41467-022-35164-x. PMID:36496453[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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