Evidence map›Paper›PMID 17592127›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Fas-activated serine/threonine phosphoprotein (FAST) is a regulator of alternative splicing.

Maria Simarro, David Mauger, Kirsten Rhee, Miguel A Pujana, Nancy L Kedersha, Satoshi Yamasaki, Michael E Cusick, Marc Vidal, Mariano A Garcia-Blanco, Paul Anderson

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-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

23 citing papers in PubMed, 40 citations in OpenAlex.

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  12. Role of Sam68 in post-transcriptional gene regulation.International journal of molecular sciences · 2013
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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 5 institutions in 2 countries.

Maria SimarroDivision of Rheumatology, Immunology, and Allergy, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
David Mauger
Kirsten Rhee
Miguel A Pujana
Nancy L Kedersha
Satoshi Yamasaki
Michael E Cusick
Marc Vidal
Mariano A Garcia-Blanco
Paul Anderson
Dana-Farber Cancer Institute · USHarvard University · USBrigham and Women's Hospital · USDuke Medical Center · USDuke University · US

Funding

Regulation of Alternative Splicing of FGFR2 pre-mRNAR01GM063090 · NIGMS · DUKE UNIVERSITY · PI GARCIA-BLANCO, MARIANO A. · 2001 to 2008
$2.3M
The role of FAST in immune-mediated inflammatory diseaseR01AR051472 · NIAMS · BRIGHAM AND WOMEN'S HOSPITAL · PI ANDERSON, PAUL J. · 2004 to 2008
$1.8M
Post-transcriptional regulation of TNF-alpha productionR01AI050167 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI ANDERSON, PAUL J. · 2001 to 2005
$1.7M
NIAID NIH HHS AI50167S1NIAID NIH HHS R01 AI050167NIAMS NIH HHS R01 AR051472NIAMS NIH HHS R01 AR51472NIGMS NIH HHS R01 GM063090NIGMS NIH HHS R01 GM63090
6 · The paper itself

Abstract

Fas-activated serine/threonine phosphoprotein (FAST) is a survival protein that is tethered to the outer mitochondrial membrane. In cells subjected to environmental stress, FAST moves to stress granules, where it interacts with TIA1 to modulate the process of stress-induced translational silencing. Both FAST and TIA1 are also found in the nucleus, where TIA1 promotes the inclusion of exons flanked by weak splice recognition sites such as exon IIIb of the fibroblast growth factor receptor 2 (FGFR2) mRNA. Two-hybrid interaction screens and biochemical analysis reveal that FAST binds to several alternative and constitutive splicing regulators, suggesting that FAST might participate in this process. The finding that FAST is concentrated at nuclear speckles also supports this contention. We show that FAST, like TIA1, promotes the inclusion of exon IIIb of the FGFR2 mRNA. Both FAST and TIA1 target a U-rich intronic sequence (IAS1) adjacent the 5' splice site of exon IIIb. However, unlike TIA1, FAST does not bind to the IAS1 sequence. Surprisingly, knockdown experiments reveal that FAST and TIA1 act independently of one another to promote the inclusion of exon IIIb. Mutational analysis reveals that FAST-mediated alternative splicing is separable from the survival effects of FAST. Our data reveal that nuclear FAST can regulate the splicing of FGFR2 transcripts.

Indexed as

Alternative SplicingAnimalsCell LineCell Nucleusfas ReceptorGene Expression RegulationHumansMiceProtein Serine-Threonine KinasesReceptor, Fibroblast Growth Factor, Type 2YeastsFAS protein, humanfas ReceptorFASTK protein, humanFGFR2 protein, humanProtein Serine-Threonine KinasesReceptor, Fibroblast Growth Factor, Type 2

Identifiers

PMID17592127
PMCPMC2040905
OpenAlexW2028558096

What OpenQuestion holds

Textmetadata
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.