Evidence map›Paper›PMID 19911040›Full record

ArticlePLoS genetics2009

The pivotal roles of TIA proteins in 5' splice-site selection of alu exons and across evolution.

Nurit Gal-Mark, Schraga Schwartz, Oren Ram, Eduardo Eyras, Gil Ast

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.7field-weighted citation impact, top 16% 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, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. T-Cell Intracellular Antigen 1-Like Protein in Physiology and Pathology.International journal of molecular sciences · 2022
    Review
  4. Review
  5. Article
  6. Article
  7. A novel role of U1 snRNP: Splice site selection from a distance.Biochimica et biophysica acta. Gene regulatory mechanisms · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Lessons from non-canonical splicing.Nature reviews. Genetics · 2016
    Review
  12. T-cell intracellular antigens in health and disease.Cell cycle (Georgetown, Tex.) · 2015
    Review
  13. Article
  14. Far upstream element-binding protein 1 and RNA secondary structure both mediate second-step splicing repression.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Article
  16. Article
  17. 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

5 authors at 2 institutions in 2 countries.

Nurit Gal-MarkDepartment of Human Molecular Genetics and Biochemistry, Sackler Faculty of Medicine, Tel-Aviv University, Tel Aviv, Israel.
Schraga Schwartz
Oren Ram
Eduardo Eyras
Gil Ast
Tel Aviv University · ILPompeu Fabra University · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

More than 5% of alternatively spliced internal exons in the human genome are derived from Alu elements in a process termed exonization. Alus are comprised of two homologous arms separated by an internal polypyrimidine tract (PPT). In most exonizations, splice sites are selected from within the same arm. We hypothesized that the internal PPT may prevent selection of a splice site further downstream. Here, we demonstrate that this PPT enhanced the selection of an upstream 5' splice site (5'ss), even in the presence of a stronger 5'ss downstream. Deletion of this PPT shifted selection to the stronger downstream 5'ss. This enhancing effect depended on the strength of the downstream 5'ss, on the efficiency of base-pairing to U1 snRNA, and on the length of the PPT. This effect of the PPT was mediated by the binding of TIA proteins and was dependent on the distance between the PPT and the upstream 5'ss. A wide-scale evolutionary analysis of introns across 22 eukaryotes revealed an enrichment in PPTs within approximately 20 nt downstream of the 5'ss. For most metazoans, the strength of the 5'ss inversely correlated with the presence of a downstream PPT, indicative of the functional role of the PPT. Finally, we found that the proteins that mediate this effect, TIA and U1C, and in particular their functional domains, are highly conserved across evolution. Overall, these findings expand our understanding of the role of TIA1/TIAR proteins in enhancing recognition of exons, in general, and Alu exons, in particular.

Indexed as

Evolution, MolecularAlu ElementsAnimalsComputational BiologyGenome, HumanHumansMolecular Sequence DataPhylogenyPoly(A)-Binding ProteinsPolypyrimidine Tract-Binding ProteinProtein BindingRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsSequence AlignmentT-Cell Intracellular Antigen-1Poly(A)-Binding ProteinsPolypyrimidine Tract-Binding ProteinRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsT-Cell Intracellular Antigen-1TIA1 protein, human

Identifiers

PMID19911040
PMCPMC2766253
OpenAlexW2002844327

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Registered trials

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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.