Evidence map›Paper›PMID 30531905›Full record

ArticleNature chemical biology2019

Acetylation of intrinsically disordered regions regulates phase separation.

Makoto Saito, Daniel Hess, Jan Eglinger, Anatol W Fritsch, Moritz Kreysing, Brian T Weinert, Chunaram Choudhary, Patrick Matthias

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 165 papers.

0numbers the graph read from it
0cells of the map it votes in
165citing papers in PubMed
9.5field-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

165 citing papers in PubMed, 298 citations in OpenAlex.

  1. In Vitro Assay of Bacterial RNA Helicases Liquid-Liquid Phase Separation.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
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  4. The Polymers of Life: Exploring Cellular Function Through Polymer Concepts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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105 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 3 countries.

Makoto SaitoFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.ORCID http://orcid.org/0000-0001-8619-5176
Daniel HessFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.ORCID http://orcid.org/0000-0002-1642-5404
Jan EglingerFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland.ORCID http://orcid.org/0000-0001-7234-1435
Anatol W FritschMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.ORCID http://orcid.org/0000-0003-0986-7068
Moritz KreysingMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.ORCID http://orcid.org/0000-0001-7432-3871
Brian T WeinertDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Chunaram ChoudharyDepartment of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-9863-433X
Patrick MatthiasFriedrich Miescher Institute for Biomedical Research, Basel, Switzerland. patrick.matthias@fmi.ch.ORCID http://orcid.org/0000-0002-3927-1452
Center for Systems Biology Dresden · DEFriedrich Miescher Institute · CHUniversity of Basel · CHUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Liquid-liquid phase separation (LLPS) of proteins containing intrinsically disordered regions (IDRs) has been proposed as a mechanism underlying the formation of membrane-less organelles. Tight regulation of IDR behavior is essential to ensure that LLPS only takes place when necessary. Here, we report that IDR acetylation/deacetylation regulates LLPS and assembly of stress granules (SGs), membrane-less organelles forming in response to stress. Acetylome analysis revealed that the RNA helicase DDX3X, an important component of SGs, is a novel substrate of the deacetylase HDAC6. The N-terminal IDR of DDX3X (IDR1) can undergo LLPS in vitro, and its acetylation at multiple lysine residues impairs the formation of liquid droplets. We also demonstrated that enhanced LLPS propensity through deacetylation of DDX3X-IDR1 by HDAC6 is necessary for SG maturation, but not initiation. Our analysis provides a mechanistic framework to understand how acetylation and deacetylation of IDRs regulate LLPS spatiotemporally, and impact membrane-less organelle formation in vivo.

Indexed as

AcetylationAnimalsCatalytic DomainCytoplasmic GranulesDEAD-box RNA HelicasesGene Knockout TechniquesHistone Deacetylase 6HumansIntrinsically Disordered ProteinsLysineMiceModels, TheoreticalOsmotic PressureRNA HelicasesDDX3X protein, humanDdx3x protein, mouseDEAD-box RNA HelicasesHdac6 protein, mouseHistone Deacetylase 6Intrinsically Disordered ProteinsLysineRNA Helicases

Identifiers

PMID30531905
OpenAlexW2903367686

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.