ArticleNature communications2018
Synergy between intrinsically disordered domains and structured proteins amplifies membrane curvature sensing.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
88 citing papers in PubMed.
- Visualization of membrane-stabilized SorCS2Journal of structural biology: X · 2026Article
- Article
- 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
- A balance between nucleating and elongating actin filaments controls deformation of protein condensates.Science advances · 2026Article
- Endocytic accessory proteins assemble clathrin while simultaneously destabilizing protein condensates.bioRxiv : the preprint server for biology · 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
- Mechanochemical feedback between confinement and actin crosslinking drives the shape dynamics of liquid-like droplets.Nature communications · 2026Article
- Endocytic protein AP180 assembly domain regulates synaptic vesicle size and release in Caenorhabditis elegans.PLoS biology · 2026Article
- Helical sensors of membrane saturation: Changes in orientation and curvature preference.Biophysical journal · 2025Article
- Mycobacterium tuberculosis uses intrinsically disordered, fast evolving proteins to interact with conserved host factors.Genome biology · 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
- Cellular Responses to Nanoscale Topography Mediated Through the RhoA/ROCK Pathway.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Lipid-Mediated Assembly of Biomolecular Condensates: Mechanisms, Regulation, and Therapeutic Implications.Biology · 2025Review
- The intrinsically disordered regions of organellophagy receptors are interchangeable and control organelle fragmentation, ER-phagy and mitophagy flux.Nature cell biology · 2025Article
- Epsin1 enforces a condensation-dependent checkpoint for ubiquitylated cargo during clathrin-mediated endocytosis.Nature communications · 2025Article
- Membrane bending energy selects for compact growth of protein assemblies.bioRxiv : the preprint server for biology · 2025Article
28 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
The ability of proteins to sense membrane curvature is essential to cellular function. All known sensing mechanisms rely on protein domains with specific structural features such as wedge-like amphipathic helices and crescent-shaped BAR domains. Yet many proteins that contain these domains also contain large intrinsically disordered regions. Here we report that disordered domains are themselves potent sensors of membrane curvature. Comparison of Monte Carlo simulations with in vitro and live-cell measurements demonstrates that the polymer-like behavior of disordered domains found in endocytic proteins drives them to partition preferentially to convex membrane surfaces, which place fewer geometric constraints on their conformational entropy. Further, proteins containing both structured curvature sensors and disordered regions are more than twice as curvature sensitive as their respective structured domains alone. These findings demonstrate an entropic mechanism of curvature sensing that is independent of protein structure and illustrate how structured and disordered domains can synergistically enhance curvature sensitivity.
Indexed as
Identifiers
What OpenQuestion holds
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.