ArticleThe Journal of biological chemistry2013
Kinetics of endophilin N-BAR domain dimerization and membrane interactions.
Article in The Journal of biological chemistry, 2013. 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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Who cites it
31 citing papers in PubMed.
- Bending the boundaries: the many facets of endophilin-As from membrane dynamics to disease.Cellular and molecular life sciences : CMLS · 2025Review
- Protein dimerization in 2D vs 3D: Geometric allostery enhances binding affinity.The Journal of chemical physics · 2025Article
- Purification of Recombinant Human Amphiphysin 1 and its N-BAR Domain.Bio-protocol · 2023Article
- Multivalent interactions between molecular components involved in fast endophilin mediated endocytosis drive protein phase separation.Nature communications · 2022Article
- Distinct dissociation rates of murine and human norovirus P-domain dimers suggest a role of dimer stability in virus-host interactions.Communications biology · 2022Article
- Curvature dependence of BAR protein membrane association and dissociation kinetics.Scientific reports · 2022Article
- The endophilin curvature-sensitive motif requires electrostatic guidance to recycle synaptic vesicles in vivo.Developmental cell · 2022Article
- Membrane partitioning and lipid selectivity of the N-terminal amphipathic H0 helices of endophilin isoforms.Biochimica et biophysica acta. Biomembranes · 2021Article
- Unfolding Mechanisms and Conformational Stability of the Dimeric Endophilin N-BAR Domain.ACS omega · 2021Article
- Thermodynamics and Free Energy Landscape of BAR-Domain Dimerization from Molecular Simulations.The journal of physical chemistry. B · 2021Article
- Reconstitution and real-time quantification of membrane remodeling by single proteins and protein complexes.Nature protocols · 2020Article
- Epigenetic Aspects of Engineered Nanomaterials: Is the Collateral Damage Inevitable?Frontiers in bioengineering and biotechnology · 2019Review
- Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019Review
- Insight into Cellular Uptake and Intracellular Trafficking of Nanoparticles.Nanoscale research letters · 2018Review
- Article
- Overview of the detection methods for equilibrium dissociation constantJournal of pharmaceutical analysis · 2018Review
- Opposing Kinesin and Myosin-I Motors Drive Membrane Deformation and Tubulation along Engineered Cytoskeletal Networks.Current biology : CB · 2018Article
- The Unsolved Problem of How Cells Sense Micron-Scale Curvature.Trends in biochemical sciences · 2017Review
- Cations induce shape remodeling of negatively charged phospholipid membranes.Physical chemistry chemical physics : PCCP · 2017Article
- The N-Terminal Amphipathic Helix of Endophilin Does Not Contribute to Its Molecular Curvature Generation Capacity.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The recruitment to plasma membrane invaginations of the protein endophilin is a temporally regulated step in clathrin-mediated endocytosis. Endophilin is believed to sense or stabilize membrane curvature, which in turn likely depends on the dimeric structure of the protein. The dynamic nature of the membrane association and dimerization of endophilin is thus functionally important and is illuminated herein. Using subunit exchange Förster resonance energy transfer (FRET), we determine dimer dissociation kinetics and find a dimerization equilibrium constant orders of magnitude lower than previously published values. We characterize N-BAR domain membrane association kinetics under conditions where the dimeric species predominates, by stopped flow, observing prominent electrostatic sensitivity of membrane interaction kinetics. Relative to membrane binding, we find that protein monomer/dimer species equilibrate with far slower kinetics. Complementary optical microscopy studies reveal strikingly slow membrane dissociation and an increase of dissociation rate constant for a construct lacking the amphipathic segment helix 0 (H0). We attribute the slow dissociation kinetics to higher-order protein oligomerization on the membrane. We incorporate our findings into a kinetic scheme for endophilin N-BAR membrane binding and find a significant separation of time scales for endophilin membrane binding and subsequent oligomerization. This separation may facilitate the regulation of membrane trafficking phenomena.
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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 OpenQuestion graph.