A widely expressed transmembrane serine/threonine kinase that does not bind activin, inhibin, transforming growth factor beta, or bone morphogenic factor.

作者: M. Kan , K. Matsuzaki , J. Xu , F. Wang , W.L. McKeehan

DOI: 10.1016/S0021-9258(18)31447-9

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摘要: Molecular cloning of complementary DNAs (cDNA) whose expression products bind activin and transforming growth factor beta (TGF-beta 1 -beta 2) suggests that transmembrane serine/threonine kinases constitute a new class signaling molecules. A human liver cell cDNA which codes for kinase receptor (SKR1) was identified using degenerate oligonucleotide primers to coding sequence mouse Caenorhabditis elegans daf-1 subdomains VI VIII in the polymerase chain reaction. The deduced 509-amino acid product consisted cysteine-rich extracellular domain cytoplasmic are 10-20 40% homologous respective domains kinases. Cells overexpressing SKR1 exhibited no increase binding activin, inhibin, TGF-beta 1, 2, or bone morphogenic type 2B. Except its absence spleen, exhibits tissue pattern similar II gene. Similarly, is expressed normal parenchymal cells, endothelial fibroblasts, tumor-derived epithelial cells. lack prototypic members 1-5 branch superfamily potentially member ligand superfamily.

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