Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12.
Transforming growth factor-beta (TGF-beta) family members bind to receptors that consist of heteromeric serine-threonine kinase subunits (type I and type II). In a yeast genetic screen, the immunophilin FKBP-12, a target of the macrolides FK506 and rapamycin, interacted with the type I receptor for TGF-beta and with other type I ... receptors. Deletion, point mutation, and co-immunoprecipitation studies further demonstrated the specificity of the interaction. Excess FK506 competed with type I receptors for binding to FKBP-12, which suggests that these receptors share or overlap the macrolide binding site on FKBP-12, and therefore they may represent its natural ligand. The specific interaction between the type I receptors and FKBP-12 suggests that FKBP-12 may play a role in type I receptor-mediated signaling.
Mesh Terms:
Binding, Competitive, Carrier Proteins, Heat-Shock Proteins, Point Mutation, Precipitin Tests, Protein-Serine-Threonine Kinases, Receptors, Transforming Growth Factor beta, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Tacrolimus, Tacrolimus Binding Proteins
Binding, Competitive, Carrier Proteins, Heat-Shock Proteins, Point Mutation, Precipitin Tests, Protein-Serine-Threonine Kinases, Receptors, Transforming Growth Factor beta, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Tacrolimus, Tacrolimus Binding Proteins
Science
Date: Jul. 29, 1994
PubMed ID: 7518616
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