Evidence map›Paper›PMID 26261210›Full record

ArticleNucleic acids research2015

TRAP150 interacts with the RNA-binding domain of PSF and antagonizes splicing of numerous PSF-target genes in T cells.

Christopher A Yarosh, Iulia Tapescu, Matthew G Thompson, Jinsong Qiu, Michael J Mallory, Xiang-Dong Fu, Kristen W Lynch

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Christopher A YaroshDepartment of Biochemistry and Biophysics Perelman, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Iulia TapescuDepartment of Biochemistry and Biophysics Perelman, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Matthew G ThompsonDepartment of Biochemistry and Biophysics Perelman, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Jinsong QiuDepartment of Cell and Molecular Medicine, University of California, San Diego, San Diego, CA 92093, USA.
Michael J MalloryDepartment of Biochemistry and Biophysics Perelman, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Xiang-Dong FuDepartment of Cell and Molecular Medicine, University of California, San Diego, San Diego, CA 92093, USA.
Kristen W LynchDepartment of Biochemistry and Biophysics Perelman, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA Department of Genetics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA klync@mail.med.upenn.edu.
University of Pennsylvania · USUniversity of California, San Diego · US

Funding

Mechanisms of Signal-Induced Alternative Splicing: CD45R01GM067719 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LYNCH, KRISTEN W · 2003 to 2015
$3.8M
Probing TRAP150/GSK3-mediated regulation of the aging-related protein PSFF31AG047022 · NIA · UNIVERSITY OF PENNSYLVANIA · PI YAROSH, CHRISTOPHER ANTHONY · 2014 to 2016
$95k
NIA NIH HHS F31 AG047022NIGMS NIH HHS R01 GM067719
6 · The paper itself

Abstract

PSF (a.k.a. SFPQ) is a ubiquitously expressed, essential nuclear protein with important roles in DNA damage repair and RNA biogenesis. In stimulated T cells, PSF binds to and suppresses the inclusion of CD45 exon 4 in the final mRNA; however, in resting cells, TRAP150 binds PSF and prevents access to the CD45 RNA, though the mechanism for this inhibition has remained unclear. Here, we show that TRAP150 binds a region encompassing the RNA recognition motifs (RRMs) of PSF using a previously uncharacterized, 70 residue region we have termed the PSF-interacting domain (PID). TRAP150's PID directly inhibits the interaction of PSF RRMs with RNA, which is mediated through RRM2. However, interaction of PSF with TRAP150 does not appear to inhibit the dimerization of PSF with other Drosophila Behavior, Human Splicing (DBHS) proteins, which is also dependent on RRM2. Finally, we use RASL-Seq to identify ∼40 T cell splicing events sensitive to PSF knockdown, and show that for the majority of these, PSF's effect is antagonized by TRAP150. Together these data suggest a model in which TRAP150 interacts with dimeric PSF to block access of RNA to RRM2, thereby regulating the activity of PSF toward a broad set of splicing events in T cells.

Indexed as

Alternative SplicingCell LineDNA-Binding ProteinsProtein BindingProtein Interaction Domains and MotifsPTB-Associated Splicing FactorRNARNA-Binding ProteinsT-LymphocytesTranscription FactorsDNA-Binding ProteinsPTB-Associated Splicing FactorRNARNA-Binding ProteinsTHRAP3 protein, humanTranscription Factors

Identifiers

PMID26261210
PMCPMC4605305
OpenAlexW2099233392

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.