Ligand-induced recruitment and phosphorylation of reduced TGF-beta type I receptor.
Receptors I (T beta R-I) and II (T beta R-II) of transforming growth factor-beta (TGF-beta) are components of a heteromeric complex in which receptor I requires receptor II to bind ligand, and receptor II requires receptor I to signal. We show that pretreatment of cells with low concentrations of dithiothreitol, which is known to disrupt ligand binding to T beta R-I, does not prevent interaction and complex formation between T beta R-II and T beta R-I. Nevertheless, our results demonstrate that ligand interaction with T beta R-I is able to induce high-affinity convertion to the complex formed. We also demonstrate that transphosphorylation of T beta R-I through bound T beta R-II can occur independently of ligand binding to T beta R-I.
Vivien
D
D
Laboratoire de Biochimie du Tissu Conjonctif, Chu Caen Côte de Nacre, France.
Wrana
J L
JL
D000818:Animals; D002460:Cell Line / Q000378:metabolism / Q000648:ultrastructure; D004229:Dithiothreitol / Q000494:pharmacology; D004847:Epithelial Cells; D004848:Epithelium / Q000648:ultrastructure; D008024:Ligands; D008907:Mink; D010766:Phosphorylation; D018125:Receptors, Transforming Growth Factor beta / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
D008024:Ligands; D018125:Receptors, Transforming Growth Factor beta; D004229:Dithiothreitol