Abstract
Transforming growth factor-β (TGF-β) signals by mediating the association of two distinct transmembrane serine/threonine kinase receptors, the type I (TβRI) and II (TβRII). Here, we took advantage of recombinant human TβRII extracellular domain (TβRII-ED) to analyze TGF-β/TβRII complex formation which is the initial event in the construction of a signaling complex. We found that recombinant TβRII-ED binds TGF-β3 more efficiently than TGF-β2 and therefore maintains the native TβRII binding selectivity for the different TGF-β isoforms. Biochemical analysis showed that free TβRII-ED is expressed as a monomer. Upon ligand binding, both TGF-β3 and -β2 isoforms induce homodimerization of TβRII-ED, each TGF-β subunit being able to bind one TβRII-ED molecule. These results suggested that ligand dependent receptor dimerization may be an important early step in the TGF-β signaling complex formation.
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