Abstract
Receptors I (TβR-I) and II (TβR-II) of transforming growth factor-β (TGF-β) 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 TβR-I, does not prevent interaction and complex formation between TβR-II and TβR-I. Nevertheless, our results demonstrate that ligand interaction with TβR-I is able to induce high-affinity convertion to the complex formed. We also demonstrate that transphosphorylation of TβR-I through bound TβR-II can occur independently of ligand binding to TβR-I.
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