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

Overview of attention for article published in BMC Neuroscience, November 2015
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Title
Novel transcripts reveal a complex structure of the human TRKA gene and imply the presence of multiple protein isoforms
Published in
BMC Neuroscience, November 2015
DOI 10.1186/s12868-015-0215-x
Pubmed ID
Authors

Kristi Luberg, Rahel Park, Elina Aleksejeva, Tõnis Timmusk

Abstract

Tropomyosin-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. We 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. Results 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.

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Geographical breakdown

Country Count As %
Unknown 40 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 12 30%
Student > Bachelor 8 20%
Researcher 7 18%
Student > Master 2 5%
Student > Doctoral Student 1 3%
Other 4 10%
Unknown 6 15%
Readers by discipline Count As %
Agricultural and Biological Sciences 11 28%
Biochemistry, Genetics and Molecular Biology 8 20%
Medicine and Dentistry 6 15%
Neuroscience 4 10%
Pharmacology, Toxicology and Pharmaceutical Science 3 8%
Other 2 5%
Unknown 6 15%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 18 November 2015.
All research outputs
#20,296,405
of 22,833,393 outputs
Outputs from BMC Neuroscience
#1,055
of 1,245 outputs
Outputs of similar age
#323,630
of 386,425 outputs
Outputs of similar age from BMC Neuroscience
#34
of 45 outputs
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