Evidence map›Paper›PMID 25940628›Full record

ArticleNucleic acids research2015

Generation of functionally distinct isoforms of PTBP3 by alternative splicing and translation initiation.

Lit-Yeen Tan, Peter Whitfield, Miriam Llorian, Elisa Monzon-Casanova, Manuel D Diaz-Munoz, Martin Turner, Christopher W J Smith

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 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 40 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Molecular Basis of Intron Retention inInternational journal of molecular sciences · 2025
    Article
  4. PTBP1 and Cancer: From RNA Regulation to Therapeutic Potential.Journal of cellular and molecular medicine · 2025
    Review
  5. Evaluation of Eukaryotic mRNA Coding Potential.Methods in molecular biology (Clifton, N.J.) · 2025
    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

7 authors at 2 institutions in 1 country.

Lit-Yeen TanDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
Peter WhitfieldDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
Miriam LlorianDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
Elisa Monzon-CasanovaDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK Laboratory of Lymphocyte Signalling and Development, The Babraham Institute, Babraham Research Campus, CB22 3AT, UK.
Manuel D Diaz-MunozLaboratory of Lymphocyte Signalling and Development, The Babraham Institute, Babraham Research Campus, CB22 3AT, UK.
Martin TurnerLaboratory of Lymphocyte Signalling and Development, The Babraham Institute, Babraham Research Campus, CB22 3AT, UK.
Christopher W J SmithDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK cwjs1@cam.ac.uk.
University of Cambridge · GBBabraham Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J001457/1Biotechnology and Biological Sciences Research Council BB/J00152X/1Biotechnology and Biological Sciences Research Council BBS/E/B/000C0407Medical Research CouncilWellcome Trust 092900
6 · The paper itself

Abstract

Polypyrimidine tract binding protein (PTBP1) is a widely expressed RNA binding protein that acts as a regulator of alternative splicing and of cytoplasmic mRNA functions. Vertebrates contain two closely-related paralogs with >75% amino acid sequence identity. Early replacement of PTBP1 by PTBP2 during neuronal differentiation causes a concerted set of splicing changes. By comparison, very little is known about the molecular functions or physiological roles of PTBP3, although its expression and conservation throughout the vertebrates suggest a role in haematopoietic cells. To begin to understand its functions we have characterized the mRNA and protein isoform repertoire of PTBP3. Combinatorial alternative splicing events at the 5' end of the gene allow for the generation of eight mRNA and three major protein isoforms. Individual mRNAs generate up to three protein isoforms via alternative translation initiation by re-initiation and leaky scanning using downstream AUG codons. The N-terminally truncated PTBP3 isoforms lack nuclear localization signals and/or most of the RRM1 domain and vary in their RNA binding properties and nuclear/cytoplasmic distribution, suggesting that PTBP3 may have major post-transcriptional cytoplasmic roles. Our findings set the stage for understanding the non-redundant physiological roles of PTBP3.

Indexed as

Alternative SplicingPeptide Chain Initiation, TranslationalAnimalsCells, CulturedCodon, InitiatorHumansK562 CellsMice, Inbred C57BLPolypyrimidine Tract-Binding ProteinProtein IsoformsRNACodon, InitiatorPolypyrimidine Tract-Binding ProteinProtein IsoformsPTBP3 protein, humanRNA

Identifiers

PMID25940628
PMCPMC4477659
OpenAlexW1819822159

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.