Evidence map›Paper›PMID 34916288›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Amphiphilic proteins coassemble into multiphasic condensates and act as biomolecular surfactants.

Fleurie M Kelley, Bruna Favetta, Roshan Mammen Regy, Jeetain Mittal, Benjamin S Schuster

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.9field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Review
  3. Redox-Dependent Chaperoning of GBF1 Condensates Regulates Seed Germination in Arabidopsis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  9. A molecular grammar for programmable multiphase protein-RNA vesicles.bioRxiv : the preprint server for biology · 2026
    Article
  10. Diverse, distinct, and densely packed DNA nanostar droplets.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  11. Review
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  18. Sequence-encoded interactions program internal condensate architecture.bioRxiv : the preprint server for biology · 2025
    Article
  19. Article
  20. Article

6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Fleurie M KelleyDepartment of Chemical and Biochemical Engineering, Rutgers, the State University of New Jersey, Piscataway, NJ 08854.
Bruna FavettaDepartment of Biomedical Engineering, Rutgers, the State University of New Jersey, Piscataway, NJ 08854.ORCID 0000-0002-3613-1665
Roshan Mammen RegyArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX 77843.
Jeetain MittalArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX 77843.ORCID 0000-0002-9725-6402
Benjamin S SchusterDepartment of Chemical and Biochemical Engineering, Rutgers, the State University of New Jersey, Piscataway, NJ 08854; bss142@soe.rutgers.edu.ORCID 0000-0002-6468-8081
Rutgers, The State University of New Jersey · USTexas A&M University · US

Funding

X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MARIUZZA, ROY A · 1998 to 2011
$32.2M
Rutgers Biotechnology Training ProgramT32GM135141 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ANN M. STOCK, Martin L Yarmush · 2020 to 2026
$3.5M
Liquid-Liquid Phase Separation in Heterochromatin OrganizationR01GM136917 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI MITTAL, JEETAIN · 2020 to 2023
$1.4M
Conformational dynamics, binding and aggregation of intrinsically disordered proteinsR01GM120537 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI VAIANA, SARA M. · 2017 to 2021
$1.4M
NCRR NIH HHS P41 RR012408NIGMS NIH HHS R01 GM120537NIGMS NIH HHS R01 GM136917NIGMS NIH HHS T32 GM135141
6 · The paper itself

Abstract

Cells contain membraneless compartments that assemble due to liquid-liquid phase separation, including biomolecular condensates with complex morphologies. For instance, certain condensates are surrounded by a film of distinct composition, such as Ape1 condensates coated by a layer of Atg19, required for selective autophagy in yeast. Other condensates are multiphasic, with nested liquid phases of distinct compositions and functions, such as in the case of ribosome biogenesis in the nucleolus. The size and structure of such condensates must be regulated for proper biological function. We leveraged a bioinspired approach to discover how amphiphilic, surfactant-like proteins may contribute to the structure and size regulation of biomolecular condensates. We designed and examined families of amphiphilic proteins comprising one phase-separating domain and one non-phase-separating domain. In particular, these proteins contain the soluble structured domain glutathione S-transferase (GST) or maltose binding protein (MBP), fused to the intrinsically disordered RGG domain from P granule protein LAF-1. When one amphiphilic protein is mixed in vitro with RGG-RGG, the proteins assemble into enveloped condensates, with RGG-RGG at the core and the amphiphilic protein forming the surface film layer. Importantly, we found that MBP-based amphiphiles are surfactants and influence droplet size, with increasing surfactant concentration resulting in smaller droplet radii. In contrast, GST-based amphiphiles at increased concentrations coassemble with RGG-RGG into multiphasic structures. We propose a mechanism for these experimental observations, supported by molecular simulations of a minimalist model. We speculate that surfactant proteins may play a significant role in regulating the structure and function of biomolecular condensates.

Indexed as

AdsorptionBiomolecular CondensatesComputer SimulationGlutathione TransferaseIntrinsically Disordered ProteinsMaltose-Binding ProteinsModels, MolecularProtein DomainsProtein MultimerizationProteinsRecombinant Fusion ProteinsSurface-Active AgentsGlutathione TransferaseIntrinsically Disordered ProteinsMaltose-Binding ProteinsProteinsRecombinant Fusion ProteinsSurface-Active Agentsintrinsically disordered proteinsliquid–liquid phase separationmolecular simulationssize regulationsurfactants

Identifiers

PMID34916288
PMCPMC8713756
OpenAlexW4226236855

What OpenQuestion holds

Textmetadata
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.