ArticleNature communications2015
Intrinsically disordered proteins drive membrane curvature.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 161 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
161 citing papers in PubMed.
- Article
- Article
- Protein Modifications for Cellular Protein Delivery.Chemical reviews · 2026Review
- Phase separation across membranes and condensates in cell organization and function.Nature reviews. Molecular cell biology · 2026Review
- Plasma membrane invaginations and their diverse cellular functions.BMC biology · 2026Review
- PMF proteins mediate mitochondrial fusion in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Endocytic accessory proteins assemble clathrin while simultaneously destabilizing protein condensates.bioRxiv : the preprint server for biology · 2026Article
- Inhibition of endocytosis by glycans arises from steric rather than electrostatic repulsion.Biophysical journal · 2026Article
- The intrinsically disordered protein SPE-56 is required for acrosomal-like exocytosis and fertility in Caenorhabditis elegans.Scientific reports · 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
- Cooperative multivalency converts disorder into rods, resolving a paradox in cellular architecture.bioRxiv : the preprint server for biology · 2026Article
- Biomolecular condensates as cellular memory modules: Thermodynamic principles and plant stress adaptation.Biophysical journal · 2026Review
- Article
- Biomolecular Condensates in and Around the ER-Golgi Interface.Sub-cellular biochemistry · 2026Review
- Poly-ubiquitylated transmembrane proteins outcompete other cargo for limited space inside clathrin-coated vesicles.Cell reports · 2025Article
- A universal entropic pulling force caused by binding.Nature communications · 2025Article
- Bending the rules: curvature's impact on cell biology.BMC biology · 2025Review
101 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
6 authors.
Funding
Abstract
Assembly of highly curved membrane structures is essential to cellular physiology. The prevailing view has been that proteins with curvature-promoting structural motifs, such as wedge-like amphipathic helices and crescent-shaped BAR domains, are required for bending membranes. Here we report that intrinsically disordered domains of the endocytic adaptor proteins, Epsin1 and AP180 are highly potent drivers of membrane curvature. This result is unexpected since intrinsically disordered domains lack a well-defined three-dimensional structure. However, in vitro measurements of membrane curvature and protein diffusivity demonstrate that the large hydrodynamic radii of these domains generate steric pressure that drives membrane bending. When disordered adaptor domains are expressed as transmembrane cargo in mammalian cells, they are excluded from clathrin-coated pits. We propose that a balance of steric pressure on the two surfaces of the membrane drives this exclusion. These results provide quantitative evidence for the influence of steric pressure on the content and assembly of curved cellular membrane structures.
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.