Evidence map›Paper›PMID 28708999›Full record

ArticleCell2017

Splicing Activation by Rbfox Requires Self-Aggregation through Its Tyrosine-Rich Domain.

Yi Ying, Xiao-Jun Wang, Celine K Vuong, Chia-Ho Lin, Andrey Damianov, Douglas L Black

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

70 citing papers in PubMed, 120 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Condensation of ZFP207 and U1 snRNP promotes spliceosome assembly.Nature structural & molecular biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. RNA-Binding Proteins in Cardiomyopathies.Journal of cardiovascular development and disease · 2024
    Review
  17. Review
  18. Review
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Yi YingMolecular Biology Interdepartmental Doctoral Program, University of California, Los Angeles, Los Angeles, CA, USA; Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA, USA.
Xiao-Jun WangDepartment of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA, USA.
Celine K VuongMolecular Biology Interdepartmental Doctoral Program, University of California, Los Angeles, Los Angeles, CA, USA; Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA, USA.
Chia-Ho LinDepartment of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA, USA.
Andrey DamianovDepartment of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA, USA.
Douglas L BlackDepartment of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA, USA; Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA, USA. Electronic address: dougb@microbio.ucla.edu.
University of California, Los Angeles · US

Funding

Mechanisms of Alternative Splicing Regulation by Rbfox ProteinsR01GM114463 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BLACK, DOUGLAS L · 2016 to 2019
$1.7M
Control of inhibitory synaptic transmission by the splicing regulator Rbfox1F31NS093923 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI VUONG, CELINE K. · 2015 to 2016
$73k
NIGMS NIH HHS R01 GM114463NINDS NIH HHS F31 NS093923
6 · The paper itself

Abstract

Proteins of the Rbfox family act with a complex of proteins called the Large Assembly of Splicing Regulators (LASR). We find that Rbfox interacts with LASR via its C-terminal domain (CTD), and this domain is essential for its splicing activity. In addition to LASR recruitment, a low-complexity (LC) sequence within the CTD contains repeated tyrosines that mediate higher-order assembly of Rbfox/LASR and are required for splicing activation by Rbfox. This sequence spontaneously aggregates in solution to form fibrous structures and hydrogels, suggesting an assembly similar to the insoluble cellular inclusions formed by FUS and other proteins in neurologic disease. Unlike the pathological aggregates, we find that assembly of the Rbfox CTD plays an essential role in its normal splicing function. Rather than simple recruitment of individual regulators to a target exon, alternative splicing choices also depend on the higher-order assembly of these regulators within the nucleus.

Indexed as

Amino Acid SequenceAnimalsBrainCytoskeletal ProteinsHumansMiceProtein DomainsRNA SplicingRNA Splicing FactorsSequence AlignmentSerine-Arginine Splicing FactorsCytoskeletal ProteinsRNA Splicing FactorsSerine-Arginine Splicing Factorsalternative splicingphase separationposttranscriptional gene regulationprotein aggregateprotein-protein interactionsRNA-binding protein

Identifiers

PMID28708999
PMCPMC5553710
OpenAlexW2735495785

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.