ArticleScience advances2023
The ins and outs of membrane bending by intrinsically disordered proteins.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Phase separation across membranes and condensates in cell organization and function.Nature reviews. Molecular cell biology · 2026Review
- Inhibition of endocytosis by glycans arises from steric rather than electrostatic repulsion.Biophysical journal · 2026Article
- Endocytic protein AP180 assembly domain regulates synaptic vesicle size and release in Caenorhabditis elegans.PLoS biology · 2026Article
- Linear ubiquitination triggers Amph-mediated T-tubule biogenesis.Science advances · 2026Article
- Mycobacterium tuberculosis uses intrinsically disordered, fast evolving proteins to interact with conserved host factors.Genome biology · 2025Article
- Condensate-membrane interactions shape membranes, tune cytoskeletal assembly, and localize mRNAs.Current opinion in cell biology · 2025Review
- Polymer sailing on rafts within lipid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Organizing principles underlying COPII-mediated transport.Current opinion in cell biology · 2025Review
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Molecular basis for the assembly of the Vps5-Vps17 SNX-BAR proteins with Retromer.Nature communications · 2025Article
- Cellular Signaling at the Nano-Bio Interface: Spotlighting Membrane Curvature.Annual review of physical chemistry · 2025Review
- Lipid packing and cholesterol content regulate membrane wetting and remodeling by biomolecular condensates.Nature communications · 2025Article
- Adhesion-driven vesicle translocation through membrane-covered pores.Biophysical journal · 2025Article
- Potential ER tubular lumen sensing by intrinsically disordered regions.Journal of cell science · 2025Article
- Biophysical modeling of membrane curvature generation and curvature sensing by the glycocalyx.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Direct computations of viscoelastic moduli of biomolecular condensates.The Journal of chemical physics · 2024Article
- Making the cut: Multiscale simulation of membrane remodeling.Current opinion in structural biology · 2024Review
- Protein condensates in the the secretory pathway: Unraveling biophysical interactions and function.Biophysical journal · 2024Review
- Coupling liquid phases in 3D condensates and 2D membranes: Successes, challenges, and tools.Biophysical journal · 2024Review
- Shaping transverse-tubules: central mechanisms that play a role in the cytosol zoning for muscle contraction.Journal of biochemistry · 2024Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Membrane curvature is essential to diverse cellular functions. While classically attributed to structured domains, recent work illustrates that intrinsically disordered proteins are also potent drivers of membrane bending. Specifically, repulsive interactions among disordered domains drive convex bending, while attractive interactions drive concave bending, creating membrane-bound, liquid-like condensates. How might disordered domains that contain both repulsive and attractive domains affect curvature? Here, we examined chimeras that combined attractive and repulsive interactions. When the attractive domain was closer to the membrane, its condensation amplified steric pressure among repulsive domains, leading to convex curvature. In contrast, when the repulsive domain was closer to the membrane, attractive interactions dominated, resulting in concave curvature. Further, a transition from convex to concave curvature occurred with increasing ionic strength, which reduced repulsion while enhancing condensation. In agreement with a simple mechanical model, these results illustrate a set of design rules for membrane bending by disordered proteins.
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