ArticleScientific reports2017
Salt Bridge Formation between the I-BAR Domain and Lipids Increases Lipid Density and Membrane Curvature.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- N6-methyladenosine RNA modified BAIAP2L2 facilitates extracellular vesicles-mediated chemoresistance transmission in gastric cancer.Journal of translational medicine · 2025Article
- Molecular Dynamics Reveal Key Steps in BAR-Related Membrane Remodeling.Pathogens (Basel, Switzerland) · 2024Article
- Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.The Journal of membrane biology · 2022Review
- Mechanism of negative membrane curvature generation by I-BAR domains.Structure (London, England : 1993) · 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
- Curvature induction and sensing of the F-BAR protein Pacsin1 on lipid membranes via molecular dynamics simulations.Scientific reports · 2019Article
- Shape transition from elliptical to cylindrical membrane tubes induced by chiral crescent-shaped protein rods.Scientific reports · 2019Article
- Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes.Biophysical journal · 2019Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Organizing membrane-curving proteins: the emerging dynamical picture.Current opinion in structural biology · 2018Review
- Biophysics of membrane curvature remodeling at molecular and mesoscopic lengthscales.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
- The Unsolved Problem of How Cells Sense Micron-Scale Curvature.Trends in biochemical sciences · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The BAR domain superfamily proteins sense or induce curvature in membranes. The inverse-BAR domain (I-BAR) is a BAR domain that forms a straight "zeppelin-shaped" dimer. The mechanisms by which IRSp53 I-BAR binds to and deforms a lipid membrane are investigated here by all-atom molecular dynamics simulation (MD), binding energy analysis, and the effects of mutation experiments on filopodia on HeLa cells. I-BAR adopts a curved structure when crystallized, but adopts a flatter shape in MD. The binding of I-BAR to membrane was stabilized by ~30 salt bridges, consistent with experiments showing that point mutations of the interface residues have little effect on the binding affinity whereas multiple mutations have considerable effect. Salt bridge formation increases the local density of lipids and deforms the membrane into a concave shape. In addition, the point mutations that break key intra-molecular salt bridges within I-BAR reduce the binding affinity; this was confirmed by expressing these mutants in HeLa cells and observing their effects. The results indicate that the stiffness of I-BAR is important for membrane deformation, although I-BAR does not act as a completely rigid template.
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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 OpenQuestion graph.