Abstract: |
Transforming growth factor β (TGFβ) and activin each bind to pairs of membrane proteins, known as receptor types I and II, that associate to form a signaling complex. We report that TSR-I and ActR-I, two human transmembrane serine/threonine kinases distantly related to TGFβ and activin type II receptors, act as type I receptors for these factors. TSR-I is a type I receptor shared by TGFβ and activin, whereas ActR-I is an activin type I receptor. ActR-I, but not TSR-I, signals a particular transcriptional response in concert with activin type II receptors. The results indicate that type I receptors are transmembrane protein kinases that associate with type II receptors to generate diverse heteromeric serine/threonine kinase complexes of different signaling capacities. © 1993. |
Keywords: |
signal transduction; controlled study; human cell; nonhuman; comparative study; binding affinity; animal cell; transforming growth factor beta; animalia; gene expression regulation; cloning, molecular; molecular sequence data; sequence homology, amino acid; species specificity; rna, messenger; sequence alignment; protein-serine-threonine kinases; membrane protein; protein transport; receptors, transforming growth factor beta; ligands; dna primers; membrane transport; receptor binding; dna, complementary; receptors, cell surface; receptors, growth factor; activin; activins; human; priority journal; article; inhibins; support, non-u.s. gov't; support, u.s. gov't, non-p.h.s.; macromolecular systems; activin receptors
|