ArticleStructure (London, England : 1993)2014
Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed.
- Structures of EHD2 filaments on curved membranes provide a model for caveolar neck stabilization.Nature communications · 2026Article
- Comparative proteomic analysis indicates differential responses to fumonisin BMycotoxin research · 2025Article
- Therapeutic avenues in bone repair: Harnessing an anabolic osteopeptide, PEPITEM, to boost bone growth and prevent bone loss.Cell reports. Medicine · 2024Article
- Identification of drug-like molecules targeting the ATPase activity of dynamin-like EHD4.PloS one · 2024Article
- Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments.Nature communications · 2022Article
- Differential requirements for the Eps15 homology domain proteins EHD4 and EHD2 in the regulation of mammalian ciliogenesis.Traffic (Copenhagen, Denmark) · 2022Article
- Article
- Subcellular trafficking and endocytic recycling of KAmerican journal of physiology. Cell physiology · 2022Review
- 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
- 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
- Keeping in touch with the membrane; protein- and lipid-mediated confinement of caveolae to the cell surface.Biochemical Society transactions · 2020Review
- Article
- Energy and Dynamics of Caveolae Trafficking.Frontiers in cell and developmental biology · 2020Review
- Cardiomyocyte damage control in heart failure and the role of the sarcolemma.Journal of muscle research and cell motility · 2019Article
- EHD2 regulates adipocyte function and is enriched at cell surface-associated lipid droplets in primary human adipocytes.Molecular biology of the cell · 2019Article
- eNOS-NO-induced small blood vessel relaxation requires EHD2-dependent caveolae stabilization.PloS one · 2019Article
- ATP-dependent membrane remodeling links EHD1 functions to endocytic recycling.Nature communications · 2018Article
- Role of the EHD Family of Endocytic Recycling Regulators for TCR Recycling and T Cell Function.Journal of immunology (Baltimore, Md. : 1950) · 2018Article
- Dynamin-Like Proteins Are Potentially Involved in Membrane Dynamics within Chloroplasts and Cyanobacteria.Frontiers in plant science · 2018Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
The dynamin-related Eps15-homology domain-containing protein 2 (EHD2) is a membrane-remodeling ATPase that regulates the dynamics of caveolae. Here, we established an electron paramagnetic resonance (EPR) approach to characterize structural features of membrane-bound EHD2. We show that residues at the tip of the helical domain can insert into the membrane and may create membrane curvature by a wedging mechanism. Using EPR and X-ray crystallography, we found that the N terminus is folded into a hydrophobic pocket of the GTPase domain in solution and can be released into the membrane. Cryoelectron microscopy demonstrated that the N terminus is not essential for oligomerization of EHD2 into a membrane-anchored scaffold. Instead, we found a function of the N terminus in regulating targeting and stable association of EHD2 to caveolae. Our data uncover an unexpected, membrane-induced regulatory switch in EHD2 and demonstrate the versatility of EPR to study structure and function of dynamin superfamily proteins.
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Registered trials
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