Evidence map›Paper›PMID 19586903›Full record

ArticleThe Journal of biological chemistry2009

The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the nuclear export receptor NXF1.

Hiroaki Uranishi, Andrei S Zolotukhin, Susan Lindtner, Soren Warming, Gen-Mu Zhang, Jenifer Bear, Neal G Copeland, Nancy A Jenkins, George N Pavlakis, Barbara K Felber

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

43 citing papers in PubMed, 52 citations in OpenAlex.

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  16. RNA Regulators in Leukemia and Lymphoma.Cold Spring Harbor perspectives in medicine · 2020
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  17. Article
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  19. The mBiochimica et biophysica acta. Gene regulatory mechanisms · 2019
    Review
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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

10 authors at 6 institutions in 2 countries.

Hiroaki UranishiHuman Retrovirus Section, Center for Cancer Research, NCI, National Institutes of Health, Frederick, Maryland 21702-1201, USA.
Andrei S Zolotukhin
Susan Lindtner
Soren Warming
Gen-Mu Zhang
Jenifer Bear
Neal G Copeland
Nancy A Jenkins
George N Pavlakis
Barbara K Felber
Center for Cancer Research · USInstitut de Recherche Vaccinale · FRThe Retina Center · USFrederick National Laboratory for Cancer Research · USNational Institutes of Health · USOrganogenesis (United States) · US

Funding

Heterodimeric IL-15 in Cancer ImmunotherapyZIABC010750 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI PAVLAKIS, GEORGE N. · 2009 to 2022
$15.6M
Posttranscriptional control of gene expressionZIABC010334 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI FELBER, BARBARA K · 2009 to 2025
$15.1M
Posttranscriptional control of gene expressionZ01BC010334 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI FELBER, BARBARA K · 2000 to 2008
$1.6M
HIV Molecular Biology and Pathogenic Mechanisms of AIDSZ01BC010750 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI PAVLAKIS, GEORGE N. · 2006 to 2008
$919k
Intramural NIH HHS
6 · The paper itself

Abstract

The human SPEN family proteins SHARP, RBM15/OTT1, and RBM15B/OTT3 share the structural domain architecture but show distinct functional properties. Here, we examined the function of OTT3 and compared it with its paralogues RBM15 and SHARP. We found that OTT3, like RBM15, has post-transcriptional regulatory activity, whereas SHARP does not, supporting a divergent role of RBM15 and OTT3. OTT3 shares with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF. Mutational analysis revealed direct interaction of OTT3 and RBM15 with NXF1 via their C-terminal regions. Biochemical and subcellular localization studies showed that OTT3 and RBM15 also interact with each other in vivo, further supporting a shared function. Genetic knockdown of RBM15 in mouse is embryonically lethal, indicating that OTT3 cannot compensate for the RBM15 loss, which supports the notion that these proteins, in addition to sharing similar activities, likely have distinct biological roles.

Indexed as

Active Transport, Cell NucleusAmino Acid MotifsAnimalsHeLa CellsHumansMiceNuclear EnvelopeNucleocytoplasmic Transport ProteinsRNA-Binding ProteinsStructural Homology, ProteinNucleocytoplasmic Transport ProteinsNXF1 protein, humanRBM15B protein, humanRBM15 protein, humanRbm15 protein, mouseRNA-Binding Proteins

Identifiers

PMID19586903
PMCPMC2758010
OpenAlexW2039487390

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.