Genomic structure and cloned cDNAs predict that four variants in the kinase domain of serine/threonine kinase receptors arise by alternative splicing and poly(A) addition

Jianming Xu, Koichi Matsuzaki, Kerstin Mckeehan, Fen Wang, Mikio Kan, Wallace L. Mckeehan

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

Heterodimers of types I and II serine/threonine kinase receptor monomers compose the active receptor complex for ligands of the transforming growth factor β family. Here we show that the genomic organization of coding sequences for the intracellular domain of a widely expressed type I serine/threonine kinase receptor is similar to that of the activin type II receptor gene. The genomic structure and cDNA clones indicate that poly(A) addition to alternative exons at each of three carboxyl-terminal coding exon- intron junctions may be a common feature of both type I and II receptor genes. The predicted products are monomers truncated at kinase subdomains VII, IX, and X which vary in kinase activity and potential serine, threonine, and tyrosine phosphorylation sites. These results suggest that combinations of variants that affect the signal-transducing intracellular kinase domain of both type I and II receptor monomers within the transforming growth factor β ligand family may add to the heterogeneity of biological effects of individual ligands in the family.

Original languageEnglish (US)
Pages (from-to)7957-7961
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue number17
DOIs
StatePublished - Aug 16 1994
Externally publishedYes

Keywords

  • activin
  • dimerization
  • hepatoma cells
  • signal transduction
  • transforming growth factor β receptor

ASJC Scopus subject areas

  • General

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