Evidence map›Paper›PMID 25775092›Full record

ArticlePLoS genetics2015

Nab3 facilitates the function of the TRAMP complex in RNA processing via recruitment of Rrp6 independent of Nrd1.

Milo B Fasken, R Nicholas Laribee, Anita H Corbett

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Substrate selectivity by the exonuclease Rrp6p.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. The multitasking polyA tail: nuclear RNA maturation, degradation and export.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  15. Controlling nuclear RNA levels.Nature reviews. Genetics · 2018
    Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article
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

3 authors at 2 institutions in 1 country.

Milo B FaskenDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, United States of America.
R Nicholas LaribeeDepartment of Pathology and Laboratory Medicine and Center for Adult Cancer Research,University of Tennessee Health Science Center, Memphis, Tennessee, United States of America.
Anita H CorbettDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, United States of America.
Emory University · USUniversity of Tennessee Health Science Center · US

Funding

MOLECULAR BASIS OF RAN MEDIATED NUCLEAR TRANSPORTR01GM058728 · NIGMS · EMORY UNIVERSITY · PI CORBETT, ANITA H. · 1999 to 2016
$5.4M
Mechanisms of transcription coregulator usage by the target of rapamycin pathwayR01GM107040 · NIGMS · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI LARIBEE, RONALD · 2013 to 2017
$1.4M
NIGMS NIH HHS GM058728NIGMS NIH HHS GM107040-01NIGMS NIH HHS R01 GM058728NIGMS NIH HHS R01 GM107040
6 · The paper itself

Abstract

Non-coding RNAs (ncRNAs) play critical roles in gene regulation. In eukaryotic cells, ncRNAs are processed and/or degraded by the nuclear exosome, a ribonuclease complex containing catalytic subunits Dis3 and Rrp6. The TRAMP (Trf4/5-Air1/2-Mtr4 polyadenylation) complex is a critical exosome cofactor in budding yeast that stimulates the exosome to process/degrade ncRNAs and human TRAMP components have recently been identified. Importantly, mutations in exosome and exosome cofactor genes cause neurodegenerative disease. How the TRAMP complex interacts with other exosome cofactors to orchestrate regulation of the exosome is an open question. To identify novel interactions of the TRAMP exosome cofactor, we performed a high copy suppressor screen of a thermosensitive air1/2 TRAMP mutant. Here, we report that the Nab3 RNA-binding protein of the Nrd1-Nab3-Sen1 (NNS) complex is a potent suppressor of TRAMP mutants. Unlike Nab3, Nrd1 and Sen1 do not suppress TRAMP mutants and Nrd1 binding is not required for Nab3-mediated suppression of TRAMP suggesting an independent role for Nab3. Critically, Nab3 decreases ncRNA levels in TRAMP mutants, Nab3-mediated suppression of air1/2 cells requires the nuclear exosome component, Rrp6, and Nab3 directly binds Rrp6. We extend this analysis to identify a human RNA binding protein, RALY, which shares identity with Nab3 and can suppress TRAMP mutants. These results suggest that Nab3 facilitates TRAMP function by recruiting Rrp6 to ncRNAs for processing/degradation independent of Nrd1. The data raise the intriguing possibility that Nab3 and Nrd1 can function independently to recruit Rrp6 to ncRNA targets, providing combinatorial flexibility in RNA processing.

Indexed as

Cell NucleusExosome Multienzyme Ribonuclease ComplexGene Expression Regulation, FungalHumansNuclear ProteinsPolyadenylationRNA-Binding ProteinsRNA, UntranslatedSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSerine EndopeptidasesExosome Multienzyme Ribonuclease ComplexNAB3 protein, S cerevisiaeNRD1 protein, S cerevisiaeNuclear ProteinsRNA-Binding ProteinsRNA, UntranslatedRRP6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSerine Endopeptidasestunicate retinoic acid-inducible modular protease

Identifiers

PMID25775092
PMCPMC4361618
OpenAlexW2034975402

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.