Evidence map›Paper›PMID 33558506›Full record

ArticleNature communications2021

Sequence-encoded and composition-dependent protein-RNA interactions control multiphasic condensate morphologies.

Taranpreet Kaur, Muralikrishna Raju, Ibraheem Alshareedah, Richoo B Davis, Davit A Potoyan, Priya R Banerjee

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed
–field-weighted citation impact
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

142 citing papers in PubMed.

  1. Review
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  10. Physics-guided design of intrinsically disordered proteins.bioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Review
  13. A molecular grammar for programmable multiphase protein-RNA vesicles.bioRxiv : the preprint server for biology · 2026
    Article
  14. Article
  15. Diverse, distinct, and densely packed DNA nanostar droplets.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  16. Article
  17. Article
  18. Article
  19. Internal Phase Separation in Synthetic DNA Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  20. Article

82 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

6 authors.

Taranpreet KaurDepartment of Physics, University at Buffalo, Buffalo, NY, USA.
Muralikrishna Raju *Department of Chemistry, Iowa State University, Ames, IA, USA.ORCID http://orcid.org/0000-0003-0386-1917
Ibraheem Alshareedah *Department of Physics, University at Buffalo, Buffalo, NY, USA.
Richoo B DavisDepartment of Physics, University at Buffalo, Buffalo, NY, USA.ORCID http://orcid.org/0000-0003-3428-3646
Davit A PotoyanDepartment of Chemistry, Iowa State University, Ames, IA, USA. potoyan@iastate.edu.
Priya R BanerjeeDepartment of Physics, University at Buffalo, Buffalo, NY, USA. prbanerj@buffalo.edu.ORCID http://orcid.org/0000-0002-6169-1461

Funding

Quantifying Physiologic and Pathologic Viscoelastic Phases of Biomolecular Condensates by Correlative Force and Fluorescence MicroscopyR35GM138186 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI BANERJEE, PRIYA R. · 2020 to 2025
$4.4M
Multi-scale computational investigation of functions and mechanisms of protein-RNA phase separation.R35GM138243 · NIGMS · IOWA STATE UNIVERSITY · PI Davit POTOYAN · 2020 to 2026
$2.4M
NIGMS NIH HHS R35 GM138186NIGMS NIH HHS R35 GM138243
6 · The paper itself

Abstract

Multivalent protein-protein and protein-RNA interactions are the drivers of biological phase separation. Biomolecular condensates typically contain a dense network of multiple proteins and RNAs, and their competing molecular interactions play key roles in regulating the condensate composition and structure. Employing a ternary system comprising of a prion-like polypeptide (PLP), arginine-rich polypeptide (RRP), and RNA, we show that competition between the PLP and RNA for a single shared partner, the RRP, leads to RNA-induced demixing of PLP-RRP condensates into stable coexisting phases-homotypic PLP condensates and heterotypic RRP-RNA condensates. The morphology of these biphasic condensates (non-engulfing/ partial engulfing/ complete engulfing) is determined by the RNA-to-RRP stoichiometry and the hierarchy of intermolecular interactions, providing a glimpse of the broad range of multiphasic patterns that are accessible to these condensates. Our findings provide a minimal set of physical rules that govern the composition and spatial organization of multicomponent and multiphasic biomolecular condensates.

Indexed as

Amino Acid SequenceArginineBase SequencePeptidesPrionsRNARNA-Binding ProteinsSurface TensionArgininePeptidesPrionsRNARNA-Binding Proteins

Identifiers

PMID33558506
PMCPMC7870978

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Registered trials

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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.