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9RBU

Cryo-ET structure of full-length membrane-bound EHD2 complex

Summary for 9RBU
Entry DOI10.2210/pdb9rbu/pdb
EMDB information53909 53911
DescriptorEH domain-containing protein 2, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION (3 entities in total)
Functional Keywordseps15-homology domain-containing proteins (ehds), dynamin-related atpases, membrane remodeling, human myotubes, membrane repair process, caveolae, ehd2, lipid homeostasis, plasma membrane invaginations, oligomer, nucleotide binding, ehd2-dependent caveolae stabilization, gtpase (g-) domain, atpase activity, liposome tubulation, structural protein
Biological sourceMus musculus (house mouse)
Total number of polymer chains4
Total formula weight247235.62
Authors
Vazquez-Sarandeses, E.,Mikirtumov, V.,Noel, J.,Kudryashev, M.,Daumke, O. (deposition date: 2025-05-27, release date: 2026-07-08, Last modification date: 2026-08-19)
Primary citationVazquez-Sarandeses, E.,Mikirtumov, V.,Noel, J.K.,Kudryashev, M.,Daumke, O.
Structures of EHD2 filaments on curved membranes provide a model for caveolar neck stabilization.
Nat Commun, 17:-, 2026
Cited by
PubMed Abstract: Caveolae are flask-shaped invaginations of the plasma membrane serving critical functions in mechano-protection and signal transduction. Caveolar dynamics, such as caveolar movement within the plasma membrane or endocytosis, relies on precise shaping of the highly curved caveolar necks. The dynamin-like EHD2 ATPase is proposed to oligomerize around the caveolar neck, but its detailed molecular action is poorly understood. Here, we employ cryo-electron tomography to elucidate structures of ring-like EHD2 filaments on tubulated liposomes. EHD2 forms highly curved membrane scaffolds which stabilize a tubular membrane geometry with undulations along the tube's axis, resembling caveolar neck architecture. An amino-terminal sequence facilitates this geometry by acting as a spacer between adjacent filaments. Moreover, in endothelial cells lacking EHD2, caveolar necks become narrower and more elongated. Our structural work provides the molecular framework for understanding EHD2 scaffold formation and its cellular function in caveolar dynamics.
PubMed: 42538327
DOI: 10.1038/s41467-026-76288-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6.7 Å)
Structure validation

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