ArticleProceedings of the National Academy of Sciences of the United States of America2017
Structural insights into the activation mechanism of dynamin-like EHD ATPases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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Who cites it
30 citing papers in PubMed, 43 citations in OpenAlex.
- Structures of EHD2 filaments on curved membranes provide a model for caveolar neck stabilization.Nature communications · 2026Article
- Structural and functional characterization of the brain-specific dynamin superfamily member RNF112.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Assembly and fission of tubular carriers mediating protein sorting in endosomes.Nature reviews. Molecular cell biology · 2024Review
- Identification of drug-like molecules targeting the ATPase activity of dynamin-like EHD4.PloS one · 2024Article
- GTP-stimulated membrane fission by the N-BAR protein AMPH-1.Traffic (Copenhagen, Denmark) · 2023Article
- Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments.Nature communications · 2022Article
- The molecular organization of differentially curved caveolae indicates bendable structural units at the plasma membrane.Nature communications · 2022Article
- Article
- The importance of caveolin as a target in the prevention and treatment of diabetic cardiomyopathy.Frontiers in immunology · 2022Review
- Lysine acetylation regulates the interaction between proteins and membranes.Nature communications · 2021Article
- Genome-wide association study reveals novel loci associated with feeding behavior in Pekin ducks.BMC genomics · 2021Article
- Cellular functions and intrinsic attributes of the ATP-binding Eps15 homology domain-containing proteins.Protein science : a publication of the Protein Society · 2020Review
- Caveolae and lipid sorting: Shaping the cellular response to stress.The Journal of cell biology · 2020Review
- EHD2-mediated restriction of caveolar dynamics regulates cellular fatty acid uptake.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Sorting nexin 17 (SNX17) links endosomal sorting to Eps15 homology domain protein 1 (EHD1)-mediated fission machinery.The Journal of biological chemistry · 2020Article
- Keeping in touch with the membrane; protein- and lipid-mediated confinement of caveolae to the cell surface.Biochemical Society transactions · 2020Review
- Functions of Vertebrate Ferlins.Cells · 2020Review
- FERARI is required for Rab11-dependent endocytic recycling.Nature cell biology · 2020Article
- Energy and Dynamics of Caveolae Trafficking.Frontiers in cell and developmental biology · 2020Review
- Distribution, dynamics and functional roles of phosphatidylserine within the cell.Cell communication and signaling : CCS · 2019Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Eps15 (epidermal growth factor receptor pathway substrate 15)-homology domain containing proteins (EHDs) comprise a family of dynamin-related mechano-chemical ATPases involved in cellular membrane trafficking. Previous studies have revealed the structure of the EHD2 dimer, but the molecular mechanisms of membrane recruitment and assembly have remained obscure. Here, we determined the crystal structure of an amino-terminally truncated EHD4 dimer. Compared with the EHD2 structure, the helical domains are 50° rotated relative to the GTPase domain. Using electron paramagnetic spin resonance (EPR), we show that this rotation aligns the two membrane-binding regions in the helical domain toward the lipid bilayer, allowing membrane interaction. A loop rearrangement in GTPase domain creates a new interface for oligomer formation. Our results suggest that the EHD4 structure represents the active EHD conformation, whereas the EHD2 structure is autoinhibited, and reveal a complex series of domain rearrangements accompanying activation. A comparison with other peripheral membrane proteins elucidates common and specific features of this activation mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.