ArticleBiophysical journal2019
Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes.
Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- The LOK C-terminus is an IBAR-like domain that facilitates membrane binding and ezrin colocalization.Biophysical journal · 2026Article
- Article
- MSBack: Multiscale Backmapping of Highly Coarse-Grained Proteins Using Constrained Diffusion.Journal of chemical theory and computation · 2025Article
- Distinct Bin/Amphiphysin/Rvs (BAR) family proteins may assemble on the same tubule to regulate membrane organizationHeliyon · 2024Article
- Sensing their plasma membrane curvature allows migrating cells to circumvent obstacles.Nature communications · 2023Article
- A NanoCurvS platform for quantitative and multiplex analysis of curvature-sensing proteins.Biomaterials science · 2023Article
- Two-dimensional molecular condensation in cell signaling and mechanosensing.Acta biochimica et biophysica Sinica · 2023Review
- Macrophages modulate stiffness-related foreign body responses through plasma membrane deformation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Activated I-BAR IRSp53 clustering controls the formation of VASP-actin-based membrane protrusions.Science advances · 2022Article
- Curvature dependence of BAR protein membrane association and dissociation kinetics.Scientific reports · 2022Article
- Molecular Shape Solution for Mesoscopic Remodeling of Cellular Membranes.Annual review of biophysics · 2022Review
- Mechanism of negative membrane curvature generation by I-BAR domains.Structure (London, England : 1993) · 2021Article
- Physical Characterization of Triolein and Implications for Its Role in Lipid Droplet Biogenesis.The journal of physical chemistry. B · 2021Article
- Full assembly of HIV-1 particles requires assistance of the membrane curvature factor IRSp53.eLife · 2021Article
- Lipid-Composition-Mediated Forces Can Stabilize Tubular Assemblies of I-BAR Proteins.Biophysical journal · 2021Article
- Mechanisms of negative membrane curvature sensing and generation by ESCRT III subunit Snf7.Protein science : a publication of the Protein Society · 2020Article
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Authors and funding
6 authors.
Funding
Abstract
Protein-mediated membrane remodeling is a ubiquitous and critical process for proper cellular function. Inverse Bin/Amphiphysin/Rvs (I-BAR) domains drive local membrane deformation as a precursor to large-scale membrane remodeling. We employ a multiscale approach to provide the molecular mechanism of unusual I-BAR domain-driven membrane remodeling at a low protein surface concentration with near-atomistic detail. We generate a bottom-up coarse-grained model that demonstrates similar membrane-bound I-BAR domain aggregation behavior as our recent Mesoscopic Membrane with Explicit Proteins model. Together, these models bridge several length scales and reveal an aggregation behavior of I-BAR domains. We find that at low surface coverage (i.e., low bound protein density), I-BAR domains form transient, tip-to-tip strings on periodic flat membrane sheets. Inside of lipid bilayer tubules, we find linear aggregates parallel to the axis of the tubule. Finally, we find that I-BAR domains form tip-to-tip aggregates around the edges of membrane domes. These results are supported by in vitro experiments showing low curvature bulges surrounded by I-BAR domains on giant unilamellar vesicles. Overall, our models reveal new I-BAR domain aggregation behavior in membrane tubules and on the surface of vesicles at low surface concentration that add insight into how I-BAR domain proteins may contribute to certain aspects of membrane remodeling in cells.
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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.