ArticleJournal of the American Chemical Society2019
Molecular Mechanisms of Membrane Curvature Sensing by a Disordered Protein.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 97 citations in OpenAlex.
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- Cholesterol differentially regulates α-synuclein binding across membrane packing regimes.bioRxiv : the preprint server for biology · 2026Article
- Membrane Phase, Charge, and Curvature Regulate α-Synuclein Binding Dynamics.bioRxiv : the preprint server for biology · 2026Article
- Inhibition of endocytosis by glycans arises from steric rather than electrostatic repulsion.Biophysical journal · 2026Article
- The disordered and structured regions ofbioRxiv : the preprint server for biology · 2026Article
- A membrane insertion code for intrinsically disordered proteins.bioRxiv : the preprint server for biology · 2026Article
- Clathrin is an Intrinsic Driver of Membrane Fission.bioRxiv : the preprint server for biology · 2026Article
- Endocytic protein AP180 assembly domain regulates synaptic vesicle size and release in Caenorhabditis elegans.PLoS biology · 2026Article
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- Missense mutations in intrinsically disordered protein regions link pathogenicity and phase separation.The Journal of biological chemistry · 2025Article
- A combined biochemical and computational approach provides evidence for membrane remodelling by the structural scaffold of the endocytic TPLATE complex.Nature plants · 2025Article
- A universal entropic pulling force caused by binding.Nature communications · 2025Article
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.Nature communications · 2025Article
- Sparse networks of conformational fluctuations communicate signals within proteins.bioRxiv : the preprint server for biology · 2025Article
- The intrinsically disordered regions of organellophagy receptors are interchangeable and control organelle fragmentation, ER-phagy and mitophagy flux.Nature cell biology · 2025Article
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.bioRxiv : the preprint server for biology · 2025Article
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The ability of proteins to sense membrane curvature is essential for the initiation and assembly of curved membrane structures. Established mechanisms of curvature sensing rely on proteins with specific structural features. In contrast, it has recently been discovered that intrinsically disordered proteins, which lack a defined three-dimensional fold, can also be potent sensors of membrane curvature. How can an unstructured protein sense the structure of the membrane surface? Many disordered proteins that associate with membranes have two key physical features: a high degree of conformational entropy and a high net negative charge. Binding of such proteins to membrane surfaces results simultaneously in a decrease in conformational entropy and an increase in electrostatic repulsion by anionic lipids. Here we show that each of these effects gives rise to a distinct mechanism of curvature sensing. Specifically, as the curvature of the membrane increases, the steric hindrance between the disordered protein and membrane is reduced, leading to an increase in chain entropy. At the same time, increasing membrane curvature increases the average separation between anionic amino acids and lipids, creating an electrostatic preference for curved membranes. Using quantitative imaging of membrane vesicles, our results demonstrate that long disordered amino acid chains with low net charge sense curvature predominately through the entropic mechanism. In contrast, shorter, more highly charged amino acid chains rely largely on the electrostatic mechanism. These findings provide a roadmap for predicting and testing the curvature sensitivity of the large and diverse set of disordered proteins that function at cellular membranes.
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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.