Evidence map›Paper›PMID 20554526›Full record

ArticleThe Journal of biological chemistry2010

Recognition of polyadenosine RNA by the zinc finger domain of nuclear poly(A) RNA-binding protein 2 (Nab2) is required for correct mRNA 3'-end formation.

Seth M Kelly, Sara W Leung, Luciano H Apponi, Anna M Bramley, Elizabeth J Tran, Julia A Chekanova, Susan R Wente, Anita H Corbett

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

36 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  6. Review
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  8. TheeLife · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Polyadenylation and nuclear export of mRNAs.The Journal of biological chemistry · 2019
    Review
  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. Article
  16. Article
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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

8 authors at 3 institutions in 1 country.

Seth M KellyDepartments of Biochemistry, Emory University School ofMedicine, Atlanta, Georgia 30322, USA.
Sara W Leung
Luciano H Apponi
Anna M Bramley
Elizabeth J Tran
Julia A Chekanova
Susan R Wente
Anita H Corbett
Emory University · USVanderbilt University · USUniversity of Missouri–Kansas City · US

Funding

Molecular Analysis of Nuclear Pore Complex FunctionR37GM051219 · NIGMS · VANDERBILT UNIVERSITY · PI WENTE, SUSAN R. · 2010 to 2019
$5.6M
MOLECULAR BASIS OF RAN MEDIATED NUCLEAR TRANSPORTR01GM058728 · NIGMS · EMORY UNIVERSITY · PI CORBETT, ANITA H. · 1999 to 2016
$5.4M
Quantitative Analysis of Nucleocytoplasmic TraffickingR01GM065442 · NIGMS · EMORY UNIVERSITY · PI CORBETT, ANITA H. · 2003 to 2006
$1.1M
NIGMS NIH HHS R01 GM058728NIGMS NIH HHS R01 GM065442NIGMS NIH HHS R37 GM051219
6 · The paper itself

Abstract

Proteins bound to the poly(A) tail of mRNA transcripts, called poly(A)-binding proteins (Pabs), play critical roles in regulating RNA stability, translation, and nuclear export. Like many mRNA-binding proteins that modulate post-transcriptional processing events, assigning specific functions to Pabs is challenging because these processing events are tightly coupled to one another. To investigate the role that a novel class of zinc finger-containing Pabs plays in these coupled processes, we defined the mode of polyadenosine RNA recognition for the conserved Saccharomyces cerevisiae Nab2 protein and assessed in vivo consequences caused by disruption of RNA binding. The polyadenosine RNA recognition domain of Nab2 consists of three tandem Cys-Cys-Cys-His (CCCH) zinc fingers. Cells expressing mutant Nab2 proteins with decreased binding to polyadenosine RNA show growth defects as well as defects in poly(A) tail length but do not accumulate poly(A) RNA in the nucleus. We also demonstrate genetic interactions between mutant nab2 alleles and mutant alleles of the mRNA 3'-end processing machinery. Together, these data provide strong evidence that Nab2 binding to RNA is critical for proper control of poly(A) tail length.

Indexed as

AdenosineCell NucleusMutationNucleocytoplasmic Transport ProteinsPolymersProtein BindingRNA 3' Polyadenylation SignalsRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsZinc FingersAdenosineNAB2 protein, S cerevisiaeNucleocytoplasmic Transport ProteinspolyadenosinePolymersRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID20554526
PMCPMC2924000
OpenAlexW2032185656

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.