Evidence map›Paper›PMID 39455581›Full record

ArticleNature communications2024

Intermolecular energy migration via homoFRET captures the modulation in the material property of phase-separated biomolecular condensates.

Ashish Joshi, Anuja Walimbe, Snehasis Sarkar, Lisha Arora, Gaganpreet Kaur, Prince Jhandai, Dhruba Chatterjee, Indranil Banerjee, Samrat Mukhopadhyay

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
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  4. Review
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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

9 authors.

Ashish Joshi *Centre for Protein Science, Design and Engineering, Indian Institute of Science Education and Research (IISER) Mohali, Mohali, India.
Anuja Walimbe *Centre for Protein Science, Design and Engineering, Indian Institute of Science Education and Research (IISER) Mohali, Mohali, India.
Snehasis SarkarCentre for Protein Science, Design and Engineering, Indian Institute of Science Education and Research (IISER) Mohali, Mohali, India.
Lisha AroraCentre for Protein Science, Design and Engineering, Indian Institute of Science Education and Research (IISER) Mohali, Mohali, India.
Gaganpreet KaurDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Mohali, Mohali, India.
Prince JhandaiDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Mohali, Mohali, India.ORCID 0009-0001-5993-8453
Dhruba ChatterjeeCentre for Protein Science, Design and Engineering, Indian Institute of Science Education and Research (IISER) Mohali, Mohali, India.
Indranil BanerjeeDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) Mohali, Mohali, India.ORCID 0000-0002-0808-2392
Samrat MukhopadhyayCentre for Protein Science, Design and Engineering, Indian Institute of Science Education and Research (IISER) Mohali, Mohali, India. mukhopadhyay@iisermohali.ac.in.ORCID 0000-0003-1242-9958

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Physical properties of biomolecular condensates formed via phase separation of proteins and nucleic acids are associated with cell physiology and disease. Condensate properties can be regulated by several cellular factors including post-translational modifications. Here, we introduce an application of intermolecular energy migration via homo-FRET (Förster resonance energy transfer), a nanometric proximity ruler, to study the modulation in short- and long-range protein-protein interactions leading to the changes in the physical properties of condensates of fluorescently-tagged FUS (Fused in Sarcoma) that is associated with the formation of cytoplasmic and nuclear membraneless organelles. We show that homoFRET captures modulations in condensate properties of FUS by RNA, ATP, and post-translational arginine methylation. We also extend the homoFRET methodology to study the in-situ formation of cytoplasmic stress granules in mammalian cells. Our studies highlight the broad applicability of homoFRET as a potent generic tool for studying intracellular phase transitions involved in function and disease.

Indexed as

Biomolecular CondensatesFluorescence Resonance Energy TransferRNA-Binding Protein FUSAdenosine TriphosphateArginineHeLa CellsHumansMethylationProtein Processing, Post-TranslationalRNAStress GranulesAdenosine TriphosphateArginineFUS protein, humanRNARNA-Binding Protein FUS

Identifiers

PMID39455581
PMCPMC11511825

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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.