Evidence map›Paper›PMID 32302572›Full record

ArticleCell2020

RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation.

Jordina Guillén-Boixet, Andrii Kopach, Alex S Holehouse, Sina Wittmann, Marcus Jahnel, Raimund Schlüßler, Kyoohyun Kim, Irmela R E A Trussina, Jie Wang, Daniel Mateju and 13 more

Abstract read
In one paragraph

Article in Cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 574 papers.

0numbers the graph read from it
0cells of the map it votes in
574citing 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

574 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Prion-Like Protein LENG8-Mediated Nucleation Drives Stress Granule Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

23 authors.

Jordina Guillén-BoixetCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Andrii KopachMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Alex S HolehouseDepartment of Biomedical Engineering and Center for Science and Engineering of Living Systems, Washington University in St. Louis, St. Louis, MO 63130, USA; Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110, USA.
Sina WittmannMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Marcus JahnelCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany; Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Raimund SchlüßlerCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Kyoohyun KimCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Irmela R E A TrussinaCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Jie WangMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Daniel MatejuMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Ina PoserMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Shovamayee MaharanaCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Martine Ruer-GrußMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Doris RichterCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Xiaojie ZhangStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Young-Tae ChangCenter for Self-Assembly and Complexity, Institute for Basic Science, Pohang 37673, Republic of Korea; Department of Chemistry, Pohang University of Science and Technology, Pohang 37673, Republic of Korea.
Jochen GuckCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
Alf HonigmannMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Julia MahamidStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Anthony A HymanMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Rohit V PappuDepartment of Biomedical Engineering and Center for Science and Engineering of Living Systems, Washington University in St. Louis, St. Louis, MO 63130, USA.
Simon AlbertiCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany; Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany. Electronic address: simon.alberti@tu-dresden.de.
Titus M FranzmannCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stressed cells shut down translation, release mRNA molecules from polysomes, and form stress granules (SGs) via a network of interactions that involve G3BP. Here we focus on the mechanistic underpinnings of SG assembly. We show that, under non-stress conditions, G3BP adopts a compact auto-inhibited state stabilized by electrostatic intramolecular interactions between the intrinsically disordered acidic tracts and the positively charged arginine-rich region. Upon release from polysomes, unfolded mRNAs outcompete G3BP auto-inhibitory interactions, engendering a conformational transition that facilitates clustering of G3BP through protein-RNA interactions. Subsequent physical crosslinking of G3BP clusters drives RNA molecules into networked RNA/protein condensates. We show that G3BP condensates impede RNA entanglement and recruit additional client proteins that promote SG maturation or induce a liquid-to-solid transition that may underlie disease. We propose that condensation coupled to conformational rearrangements and heterotypic multivalent interactions may be a general principle underlying RNP granule assembly.

Indexed as

Carrier ProteinsCell Line, TumorCytoplasmCytoplasmic GranulesDNA HelicasesHeLa CellsHumansNucleic Acid ConformationOrganellesPhosphorylationPoly-ADP-Ribose Binding ProteinsRibonucleoproteinsRNA HelicasesRNA, MessengerRNA Recognition Motif ProteinsStress, PhysiologicalCarrier ProteinsDNA HelicasesG3BP1 protein, humanPoly-ADP-Ribose Binding ProteinsRibonucleoproteinsRNA HelicasesRNA, MessengerRNA Recognition Motif ProteinsG3BPliquid-to-solid transitionNeurodegenerative diseasephase separationRNP granulesstress granulesstress response

Identifiers

PMID32302572
PMCPMC7181197

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.