ArticleScientific reports2015
Structural insights into the cooperative remodeling of membranes by amphiphysin/BIN1.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 54 citations in OpenAlex.
- Bridging autophagy and endolysosomal dysfunction: Role of bridging integrator 1 in Alzheimer's disease.Neural regeneration research · 2026Article
- Plasma membrane invaginations and their diverse cellular functions.BMC biology · 2026Review
- GTP hydrolysis triggers membrane remodeling by AMPH-1.Science advances · 2025Article
- Assembly and fission of tubular carriers mediating protein sorting in endosomes.Nature reviews. Molecular cell biology · 2024Review
- Congenital myopathies: pathophysiological mechanisms and promising therapies.Journal of translational medicine · 2024Review
- Dynamics of membrane tubulation coupled with fission by a two-component module.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- PMIpred: a physics-informed web server for quantitative protein-membrane interaction prediction.Bioinformatics (Oxford, England) · 2024Article
- Mechanistic analysis of a novel membrane-interacting variable loop in the pleckstrin-homology domain critical for dynamin function.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Stabilization of membrane topologies by proteinaceous remorin scaffolds.Nature communications · 2023Article
- Strength in numbers: effect of protein crowding on the shape of cell membranes.Biochemical Society transactions · 2022Review
- Centronuclear Myopathy Caused by Defective Membrane Remodelling of Dynamin 2 and BIN1 Variants.International journal of molecular sciences · 2022Review
- Membrane partitioning and lipid selectivity of the N-terminal amphipathic H0 helices of endophilin isoforms.Biochimica et biophysica acta. Biomembranes · 2021Article
- Modeling membrane nanotube morphology: the role of heterogeneity in composition and material properties.Scientific reports · 2020Article
- Three members of the yeast N-BAR proteins family form heterogeneous lattices in vivo and interact differentially with two RabGAP proteins.Scientific reports · 2020Article
- Structured and intrinsically disordered domains within Amphiphysin1 work together to sense and drive membrane curvature.Soft matter · 2019Article
- Cellular Blebs and Membrane Invaginations Are Coupled through Membrane Tension Buffering.Biophysical journal · 2019Article
- A stochastic model of ion channel cluster formation in the plasma membrane.The Journal of general physiology · 2019Article
- Shape transition from elliptical to cylindrical membrane tubes induced by chiral crescent-shaped protein rods.Scientific reports · 2019Article
- ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages.PLoS computational biology · 2019Article
- Membrane Morphologies Induced by Arc-Shaped Scaffolds Are Determined by Arc Angle and Coverage.Biophysical journal · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amphiphysin2/BIN1 is a crescent-shaped N-BAR protein playing a key role in forming deeply invaginated tubes in muscle T-tubules. Amphiphysin2/BIN1 structurally stabilizes tubular formations in contrast to other N-BAR proteins involved in dynamic membrane scission processes; however, the molecular mechanism of the stabilizing effect is poorly understood. Using cryo-EM, we investigated the assembly of the amphiphysin/BIN1 on a membrane tube. We found that the N-BAR domains self-assemble on the membrane surface in a highly cooperative manner. Our biochemical assays and 3D reconstructions indicate that the N-terminal amphipathic helix H0 plays an important role in the initiation of the tube assembly and further in organizing BAR-mediated polymerization by locking adjacent N-BAR domains. Mutants that lack H0 or the tip portion, which is also involved in interactions of the neighboring BAR unit, lead to a disruption of the polymer organization, even though tubulation can still be observed. The regulatory region of amphiphysin/BIN1 including an SH3 domain does not have any apparent involvement in the polymer lattice. Our study indicates that the H0 helix and the BAR tip are necessary for efficient and organized self-assembly of amphiphysin/N-BAR.
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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.