Abstract
Transforming growth factor-β (TGF-β) 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-β 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.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 8:01 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 14, 2024, 11:03 p.m.) |
Indexed | 1 week, 6 days ago (Aug. 22, 2025, 12:47 a.m.) |
Issued | 31 years, 1 month ago (July 29, 1994) |
Published | 31 years, 1 month ago (July 29, 1994) |
Published Print | 31 years, 1 month ago (July 29, 1994) |
@article{Wang_1994, title={Specific Interaction of Type I Receptors of the TGF-β Family with the Immunophilin FKBP-12}, volume={265}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.7518616}, DOI={10.1126/science.7518616}, number={5172}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Wang, Tongwen and Donahoe, Patricia K. and Zervos, Antonis S.}, year={1994}, month=jul, pages={674–676} }