Evidence map›Paper›PMID 24789627›Full record

ReviewWiley interdisciplinary reviews. RNA

Poly(A) RNA-binding proteins and polyadenosine RNA: new members and novel functions.

Callie P Wigington, Kathryn R Williams, Michael P Meers, Gary J Bassell, Anita H Corbett

Open access · greenAbstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. RNA. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 14% 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

64 citing papers in PubMed, 1 synthesis or guideline pooled it, 105 citations in OpenAlex.

  1. Pooled it
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  19. Fluorogenic RNA-based biomaterials for imaging and tracking the cargo of extracellular vesicles.Journal of controlled release : official journal of the Controlled Release Society · 2024
    Article
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4 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

5 authors at 2 institutions in 1 country.

Callie P WigingtonDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA, USA.
Kathryn R Williams
Michael P Meers
Gary J Bassell
Anita H Corbett
Emory University · USUniversity of North Carolina at Chapel Hill · US

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
MOLECULAR BASIS OF RAN MEDIATED NUCLEAR TRANSPORTR01GM058728 · NIGMS · EMORY UNIVERSITY · PI CORBETT, ANITA H. · 1999 to 2016
$5.4M
Imaging FMRP regulation and functionR01MH085617 · NIMH · EMORY UNIVERSITY · PI BASSELL, GARY J · 2009 to 2013
$1.9M
Modulation of RhoA Signaling by the mRNA Binding Protein hnRNPQ1F31MH095266 · NIMH · EMORY UNIVERSITY · PI MOSS, KATHRYN RENAE · 2012 to 2014
$93k
A Role for the Novel Poly(A) RNA-Binding Protein, ZC3H14, in Breast CancerF31CA168321 · NCI · EMORY UNIVERSITY · PI WIGINGTON, CALLIE PREAST · 2012 to 2014
$84k
NCI NIH HHS F31 CA168321NIGMS NIH HHS R01 GM058728NIGMS NIH HHS T32 GM008367NIMH NIH HHS F31 MH095266NIMH NIH HHS R01 MH085617
6 · The paper itself

Abstract

Poly(A) RNA-binding proteins (Pabs) bind with high affinity and specificity to polyadenosine RNA. Textbook models show a nuclear Pab, PABPN1, and a cytoplasmic Pab, PABPC, where the nuclear PABPN1 modulates poly(A) tail length and the cytoplasmic PABPC stabilizes poly(A) RNA in the cytoplasm and also enhances translation. While these conventional roles are critically important, the Pab family has expanded recently both in number and in function. A number of novel roles have emerged for both PAPBPN1 and PABPC that contribute to the fine-tuning of gene expression. Furthermore, as the characterization of the nucleic acid binding properties of RNA-binding proteins advances, additional proteins that show high affinity and specificity for polyadenosine RNA are being discovered. With this expansion of the Pab family comes a concomitant increase in the potential for Pabs to modulate gene expression. Further complication comes from an expansion of the potential binding sites for Pab proteins as revealed by an analysis of templated polyadenosine stretches present within the transcriptome. Thus, Pabs could influence mRNA fate and function not only by binding to the nontemplated poly(A) tail but also to internal stretches of adenosine. Understanding the diverse functions of Pab proteins is not only critical to understand how gene expression is regulated but also to understand the molecular basis for tissue-specific diseases that occur when Pab proteins are altered. Here we describe both conventional and recently emerged functions for PABPN1 and PABPC and then introduce and discuss three new Pab family members, ZC3H14, hnRNP-Q1, and LARP4.

Indexed as

AdenosineAutoantigensBinding SitesGene Expression RegulationHeterogeneous-Nuclear RibonucleoproteinsHumansNuclear ProteinsPoly(A)-Binding Protein IPoly(A)-Binding ProteinsPolyadenylationPolymersProtein BindingProtein BiosynthesisRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerAdenosineAutoantigensHeterogeneous-Nuclear RibonucleoproteinsNuclear ProteinsPABPN1 protein, humanPoly(A)-Binding Protein IPoly(A)-Binding ProteinspolyadenosinePolymersRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSS-B AntigenSYNCRIP protein, humanZC3H14 protein, human

Identifiers

PMID24789627
PMCPMC4332543
OpenAlexW1780286989

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.