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Characterization of RET proto-oncogene 3' splicing variants and polyadenylation sites: a novel C-terminus for RET

S M Myers1, C Eng, B A Ponder

  • 1Department of Pathology, Queen's University, Kingston, ON, Canada.

Oncogene
|November 16, 1995
PubMed

Insights

Researchers identified a novel RET protein isoform by analyzing alternative splicing variants of the RET proto-oncogene. This discovery expands our understanding of RET transcript diversity and potential protein functions.

Area of Science:

  • Molecular Biology
  • Genetics
  • Oncology

Background:

  • The RET proto-oncogene encodes a receptor tyrosine kinase involved in various cellular processes.
  • Alternative splicing of RET transcripts generates diverse coding and untranslated region (UTR) sequences.
  • Previous studies reported splicing variants 3' of exon 19, but a comprehensive characterization was lacking.

Purpose of the Study:

  • To sequence the full-length RET coding region.
  • To characterize RET transcripts and 3' UTRs generated by alternative splicing.
  • To identify novel RET protein isoforms and alternative splicing events.

Main Methods:

  • Sequencing of RET cDNA from a pheochromocytoma library.
  • Reverse transcriptase PCR (RT-PCR) using RNA from a neuroblastoma cell line (LA-N-2).
  • Analysis of alternatively spliced exons and 3' UTRs downstream of exon 19.

Main Results:

  • Identification of three distinct carboxyl termini for RET, including a novel 43-amino acid form.
  • Sequencing of 3621 base pairs downstream of exon 19, revealing alternatively spliced exons and UTRs.
  • Discovery of four polyadenylation sites, suggesting the potential for up to 10 different 3' RET sequences and 40 full-length transcripts.

Conclusions:

  • A novel RET protein isoform, resulting from alternative splicing, has been identified.
  • The RET gene exhibits extensive transcript diversity due to alternative splicing of its 3' terminus and multiple polyadenylation sites.
  • This complexity in RET gene expression may contribute to its role in various cellular functions and diseases.

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