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• W1576493498 abstract "Transforming growth factors beta (TGF-beta s) are disulfide-linked dimers. In Rat-1 cells both radioiodinated TGF-beta 1 and -beta 2 bind to and can be chemically cross-linked to type I and II receptors (which are thought to mediate effects of cell growth suppression and gene activation), to type III proteoglycan receptors, and to a novel approximately 50-kDa protein. After detergent solubilization of cells that were cross-linked with radioiodinated TGF-beta, antibodies specific for the type II receptor precipitated labeled receptor types I and III as well as type II. In these cells, the type III receptor is the predominant TGF-beta-binding protein, and antibodies specific for it precipitate mainly this cross-linked receptor. Thus, in the presence of TGF-beta ligand, receptor types II and III and types II and I form heteromeric complexes. The majority of the type III receptor does not associate with receptor types I and II, probably reflecting the relative amounts of the three receptors on the surface of Rat-1 cells. Since TGF-beta 1 but not TGF-beta 2 binds to the exoplasmic domain of the type II receptor in the absence of the type III receptor, and since both TGF-beta 1 and -beta 2 bind with high affinity to the type III receptor, we suggest that TGF-beta 2, and possibly TGF-beta 1, bind initially to the type III receptor. The TGF-beta 2-type III receptor complex would then interact with a type II receptor, thus modulating the affinity of the type II receptor for TGF-beta 2." @default.
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• W1576493498 date "1993-10-01" @default.
• W1576493498 modified "2023-10-18" @default.
• W1576493498 title "The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand." @default.
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• W1576493498 doi "https://doi.org/10.1016/s0021-9258(18)41509-8" @default.
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