ArticleNature communications2026
Two-dimensional HRS condensates drive the assembly of flat clathrin lattices on endosomes.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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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.
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Who cites it
6 citing papers in PubMed.
- From Pits to Plaques: Electron Microscopy Reveals Clathrin Structural Plasticity in Trafficking, Sorting and Adhesion.Traffic (Copenhagen, Denmark) · 2026Review
- Quantification of cholesterol incorporation in giant unilamellar vesicles produced by a modified cDICE method.Soft matter · 2026Article
- Dynamics of the formation of flat clathrin lattices in response to growth factor stimulus.PLoS computational biology · 2026Article
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.Nature communications · 2025Article
- Dynamics of the formation of flat clathrin lattices in response to growth factor stimulus.bioRxiv : the preprint server for biology · 2025Article
- Of condensates and coats - reciprocal regulation of clathrin assembly and the growth of protein networks.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
In cells, the curved clathrin structures in vesicle budding are well characterized, while the flat ones remain poorly understood. Here, we reconstitute the flat assembly of ESCRT-0 protein HRS and clathrin onto lipid membranes in vitro. HRS forms gel-like protein condensates at micromolar concentrations in solutions. These condensates spread as a two-dimensional layer on negatively charged membranes and, together with clathrin, form multilayered coats. Importantly, the two-dimensional condensates spontaneously form only on membranes at HRS concentrations below 50 nM, its cytoplasmic concentration. Correlative cryo-electron tomography of HRS-labelled endosomes in cells reveals a multilayered structure containing a flat clathrin layer 16 nm away from the membrane, consistent with our in vitro findings. Cholesterol enhances HRS recruitment to the membrane both in cells and in supported bilayers. Furthermore, cholesterol promotes the phase separation of HRS onto membranes, which in turn concentrates cholesterol underneath. This positive feedback promotes the formation of HRS-clathrin microdomains that sorts reconstituted ubiquitinated cargoes. Altogether, our results show that the distinct architecture of ESCRT-0 is assembled by the two-dimensional phase-separation of HRS which drives the assembly of flat clathrin coats.
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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 Socratic graph.