Evidence map›Paper›PMID 32048997›Full record

ArticleMolecular cell2020

Arginine-Enriched Mixed-Charge Domains Provide Cohesion for Nuclear Speckle Condensation.

Jamie A Greig, Tu Anh Nguyen, Michelle Lee, Alex S Holehouse, Ammon E Posey, Rohit V Pappu, Gregory Jedd

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed
11.8field-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

148 citing papers in PubMed, 238 citations in OpenAlex.

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  14. Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026
    Article
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  19. Review
  20. YTHDC1 recognizes METTL16-dependent mProceedings of the National Academy of Sciences of the United States of America · 2026
    Article

88 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

7 authors at 3 institutions in 2 countries.

Jamie A GreigTemasek Life Sciences Laboratory and Department of Biological Sciences, The National University of Singapore, Singapore 117604, Singapore.
Tu Anh NguyenTemasek Life Sciences Laboratory and Department of Biological Sciences, The National University of Singapore, Singapore 117604, Singapore.
Michelle LeeTemasek Life Sciences Laboratory and Department of Biological Sciences, The National University of Singapore, Singapore 117604, Singapore.
Alex S HolehouseDepartment of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, MO 63130, USA.
Ammon E PoseyDepartment of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, MO 63130, USA.
Rohit V PappuDepartment of Biomedical Engineering and Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, MO 63130, USA.
Gregory JeddTemasek Life Sciences Laboratory and Department of Biological Sciences, The National University of Singapore, Singapore 117604, Singapore. Electronic address: gregory@tll.org.sg.
Temasek Life Sciences Laboratory · SGWashington University in St. Louis · USNational University of Singapore · SG

Funding

ROLE OF CHAIN LENGTH AND SEQUENCE CONTEXTS ON POLYGLUTAMINE OLIGOMERIZATIONR01NS056114 · NINDS · WASHINGTON UNIVERSITY · PI PAPPU, ROHIT V · 2007 to 2020
$4.4M
Mechanism of modulation of huntingtin exon 1 aggregation by profilinR01NS089932 · NINDS · WASHINGTON UNIVERSITY · PI DIAMOND, MARC I, LANGEN, RALF · 2016 to 2020
$2.8M
NINDS NIH HHS R01 NS056114NINDS NIH HHS R01 NS089932
6 · The paper itself

Abstract

Low-complexity protein domains promote the formation of various biomolecular condensates. However, in many cases, the precise sequence features governing condensate formation and identity remain unclear. Here, we investigate the role of intrinsically disordered mixed-charge domains (MCDs) in nuclear speckle condensation. Proteins composed exclusively of arginine-aspartic acid dipeptide repeats undergo length-dependent condensation and speckle incorporation. Substituting arginine with lysine in synthetic and natural speckle-associated MCDs abolishes these activities, identifying a key role for multivalent contacts through arginine's guanidinium ion. MCDs can synergize with a speckle-associated RNA recognition motif to promote speckle specificity and residence. MCD behavior is tunable through net-charge: increasing negative charge abolishes condensation and speckle incorporation. Contrastingly, increasing positive charge through arginine leads to enhanced condensation, speckle enlargement, decreased splicing factor mobility, and defective mRNA export. Together, these results identify key sequence determinants of MCD-promoted speckle condensation and link the dynamic material properties of speckles with function in mRNA processing.

Indexed as

ArginineCell NucleusHumansIntrinsically Disordered ProteinsLysineMutationPhosphorylationProtein DomainsRNA, MessengerRNA SplicingSerine-Arginine Splicing FactorsArginineIntrinsically Disordered ProteinsLysineRNA, MessengerSerine-Arginine Splicing Factorsbiomolecular condensateintrinsically disordered proteinlow-complexity domainmembraneless organellemixed-charge domainmRNA processingnuclear specklephase separationribonucleoprotein (RNP) bodies

Identifiers

PMID32048997
PMCPMC10715173
OpenAlexW3005839507

What OpenQuestion holds

Textmetadata
LicenceTDM
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.