Evidence map›Paper›PMID 36224177›Full record

ArticleNature communications2022

The coilin N-terminus mediates multivalent interactions between coilin and Nopp140 to form and maintain Cajal bodies.

Edward Courchaine, Sara Gelles-Watnick, Martin Machyna, Korinna Straube, Sarah Sauyet, Jade Enright, Karla M Neugebauer

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. A Novel Role for Coilin in Vertebrate Innate Immunity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Biomolecular condensates and disease pathogenesis.Science China. Life sciences · 2024
    Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023
    Review
  19. Review
  20. Review
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 1 institution in 1 country.

Edward Courchaine *Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
Sara Gelles-Watnick *Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0002-3174-784X
Martin Machyna *Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
Korinna StraubeDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
Sarah SauyetDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0003-0063-9691
Jade EnrightDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0002-5051-2288
Karla M NeugebauerDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA. karla.neugebauer@yale.edu.ORCID 0000-0002-3835-6761
Yale University · US

Funding

The second phase of NIH Common Fund 4D Nucleome Network Organizational HubU01CA200147 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZHONG, SHENG · 2015 to 2024
$22.0M
DMA-Tudor interaction modules: a novel approach to Survival Motor Neuron protein (SMN) and Cajal body functionR01NS128358 · NINDS · YALE UNIVERSITY · PI Karla M Neugebauer · 2022 to 2026
$2.2M
Cajal body assembly mechanisms in vitro and in the context of neurodegenerative diseaseF31NS105379 · NINDS · YALE UNIVERSITY · PI COURVAN, EDWARD MICHAEL COURCHAINE · 2017 to 2019
$103k
NCI NIH HHS U01 CA200147NINDS NIH HHS F31 NS105379NINDS NIH HHS R01 NS128358
6 · The paper itself

Abstract

Cajal bodies (CBs) are ubiquitous nuclear membraneless organelles (MLOs) that concentrate and promote efficient biogenesis of snRNA-protein complexes involved in splicing (snRNPs). Depletion of the CB scaffolding protein coilin disperses snRNPs, making CBs a model system for studying the structure and function of MLOs. Although it is assumed that CBs form through condensation, the biomolecular interactions responsible remain elusive. Here, we discover the unexpected capacity of coilin's N-terminal domain (NTD) to form extensive fibrils in the cytoplasm and discrete nuclear puncta in vivo. Single amino acid mutational analysis reveals distinct molecular interactions between coilin NTD proteins to form fibrils and additional NTD interactions with the nuclear Nopp140 protein to form puncta. We provide evidence that Nopp140 has condensation capacity and is required for CB assembly. From these observations, we propose a model in which coilin NTD-NTD mediated assemblies make multivalent contacts with Nopp140 to achieve biomolecular condensation in the nucleus.

Indexed as

Coiled BodiesRibonucleoproteins, Small NuclearAmino AcidsCell NucleusHeLa CellsHumansRNA, Small NuclearAmino AcidsRibonucleoproteins, Small NuclearRNA, Small Nuclear

Identifiers

PMID36224177
PMCPMC9556525
OpenAlexW4304690507

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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.