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

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 widely expressed type I serine/threonine...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1994-08, Vol.91 (17), p.7957-7961
Main Authors: Xu, Jianming, Matsuzaki, Koichi, McKeehan, Kerstin, Wang, Fen, Kan, Mikio
Format: Article
Language:English
Subjects:
Alternative Splicing
Amino Acid Sequence
Base Sequence
Carcinoma, Hepatocellular
Cell Line
Cellular biology
Cloning, Molecular
Conserved Sequence
DNA Primers
DNA, Complementary - chemistry
DNA, Complementary - metabolism
Enzymes
Gene Expression
Genetic Variation
Humans
Liver Neoplasms
Macromolecular Substances
Molecular Sequence Data
Poly A - metabolism
Polymerase Chain Reaction
Protein-Serine-Threonine Kinases - biosynthesis
Receptors, Growth Factor - biosynthesis
Receptors, Growth Factor - genetics
Receptors, Transforming Growth Factor beta
RNA, Messenger - biosynthesis
Sequence Homology, Amino Acid
Transforming Growth Factor beta - metabolism
Tumor Cells, Cultured
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Summary: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 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-intro junctions may be a common feature of both type I and II receptor genes. The predicated products are monomers truncated at kinase subdomians 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 effect 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.91.17.7957