Evidence map›Paper›PMID 26581861›Full record

ArticleBMC neuroscience2015

Novel transcripts reveal a complex structure of the human TRKA gene and imply the presence of multiple protein isoforms.

Kristi Luberg, Rahel Park, Elina Aleksejeva, Tõnis Timmusk

Open access · goldAbstract read
In one paragraph

Article in BMC neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 2 pooled it
1.1field-weighted citation impact, top 26% 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

14 citing papers in PubMed, 2 syntheses or guidelines pooled it, 24 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  7. Article
  8. Novel Gross Deletion Mutations inFrontiers in pediatrics · 2021
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  9. Review
  10. The oncogenic neurotrophin receptor tropomyosin-related kinase variant, TrkAIII.Journal of experimental & clinical cancer research : CR · 2018
    Review
  11. Article
  12. 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

4 authors at 2 institutions in 1 country.

Kristi LubergDepartment of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, 12618, Tallinn, Estonia. kristi.luberg@ttu.ee.
Rahel ParkDepartment of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, 12618, Tallinn, Estonia. rahelpark@gmail.com.
Elina AleksejevaDepartment of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, 12618, Tallinn, Estonia. eleksejeva@gmail.com.
Tõnis TimmuskDepartment of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, 12618, Tallinn, Estonia. tonis.timmusk@ttu.ee.
Tallinn University of Technology · EEVähiuuringute Tehnoloogia Arenduskeskus · EE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundTropomyosin-related kinase A (TRKA) is a nerve growth factor (NGF) receptor that belongs to the tyrosine kinase receptor family. It is critical for the correct development of many types of neurons including pain-mediating sensory neurons and also controls proliferation, differentiation and survival of many neuronal and non-neuronal cells. TRKA (also known as NTRK1) gene is a target of alternative splicing which can result in several different protein isoforms. Presently, three human isoforms (TRKAI, TRKAII and TRKAIII) and two rat isoforms (TRKA L0 and TRKA L1) have been described.

resultsWe show here that human TRKA gene is overlapped by two genes and spans 67 kb--almost three times the size that has been previously described. Numerous transcription initiation sites from eight different 5' exons and a sophisticated splicing pattern among exons encoding the extracellular part of TRKA receptor indicate that there might be a large variety of alternative protein isoforms. TrkA genes in rat and mouse appear to be considerably shorter, are not overlapped by other genes and display more straightforward splicing patterns. We describe the expression profile of alternatively spliced TRKA transcripts in different tissues of human, rat and mouse, as well as analyze putative endogenous TRKA protein isoforms in human SH-SY5Y and rat PC12 cells. We also characterize a selection of novel putative protein isoforms by portraying their phosphorylation, glycosylation and intracellular localization patterns. Our findings show that an isoform comprising mainly of TRKA kinase domain is capable of entering the nucleus.

conclusionsResults obtained in this study refer to the existence of a multitude of TRKA mRNA and protein isoforms, with some putative proteins possessing very distinct properties.

Indexed as

Tissue BanksTranscriptomeAlternative SplicingAnimalsHumansMiceProtein IsoformsRatsRats, Sprague-DawleyReceptor, trkARNA, MessengerProtein IsoformsReceptor, trkARNA, Messenger

Identifiers

PMID26581861
PMCPMC4652384
OpenAlexW2174095318

What OpenQuestion holds

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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.