Abstract: |
Transforming growth factor β (TGFβ) signals through a heteromeric protein kinase receptor that has a limited ability to bind ligand. This limitation is overcome by the action of betaglycan (TGFβ type III receptor), a separate TGFβ-binding membrane protein of previously unknown function. Betaglycan presents TGFβ directly to the kinase subunit of the signaling receptor, forming a high affinity ternary complex. Membrane betaglycan increases TGFβ binding to the signaling receptor, enhances cell responsiveness to TGFβ, and eliminates marked biological differences between TGFβ isoforms. Thus, betaglycan is a direct regulator of TGFβ access to the signaling receptors. © 1993. |
Keywords: |
signal transduction; binding affinity; models, biological; transforming growth factor beta; cell line; membrane proteins; amino acid sequence; molecular sequence data; bioassay; membrane protein; immunoprecipitation; receptors, transforming growth factor beta; ligands; base sequence; receptor affinity; protein kinase; ligand binding; phosphotransferases; fibroblast growth factor; receptor binding; membrane binding; cell surface receptor; receptors, cell surface; binding, competitive; cell receptor; proteoglycans; human; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.
|