Evidence map›Paper›PMID 35411085›Full record

ArticleNature cell biology2022

Membrane surfaces regulate assembly of ribonucleoprotein condensates.

Wilton T Snead, Ameya P Jalihal, Therese M Gerbich, Ian Seim, Zhongxiu Hu, Amy S Gladfelter

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
13.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

110 citing papers in PubMed, 162 citations in OpenAlex.

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  10. Synergistic effect of PIPBiophysical journal · 2026
    Article
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  12. MgChem & bio engineering · 2026
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50 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Wilton T SneadDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.ORCID http://orcid.org/0000-0003-1411-1281
Ameya P JalihalDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Therese M GerbichDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Ian SeimDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.ORCID http://orcid.org/0000-0001-9719-2552
Zhongxiu HuDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Amy S GladfelterDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA. amyglad@unc.edu.ORCID http://orcid.org/0000-0002-2490-6945
University of North Carolina at Chapel Hill · US

Funding

Cytoplasmic Organization by phase transitionsR01GM081506 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GLADFELTER, AMY S · 2010 to 2023
$4.0M
Regulatory mechanisms of protein and RNA phase transitionsF32GM136055 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SNEAD, WILTON THOMAS · 2020 to 2022
$201k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM136055NIGMS NIH HHS R01 GM081506
6 · The paper itself

Abstract

Biomolecular condensates organize biochemistry, yet little is known about how cells control the position and scale of these structures. In cells, condensates often appear as relatively small assemblies that do not coarsen into a single droplet despite their propensity to fuse. Here, we report that ribonucleoprotein condensates of the glutamine-rich protein Whi3 interact with the endoplasmic reticulum, which prompted us to examine how membrane association controls condensate size. Reconstitution revealed that membrane recruitment promotes Whi3 condensation under physiological conditions. These assemblies rapidly arrest, resembling size distributions seen in cells. The temporal ordering of molecular interactions and the slow diffusion of membrane-bound complexes can limit condensate size. Our experiments reveal a trade-off between locally enhanced protein concentration at membranes, which favours condensation, and an accompanying reduction in diffusion, which restricts coarsening. Given that many condensates bind endomembranes, we predict that the biophysical properties of lipid bilayers are key for controlling condensate sizes throughout the cell.

Indexed as

RibonucleoproteinsRibonucleoproteins

Identifiers

PMID35411085
PMCPMC9035128
OpenAlexW4223469611

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.