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Specific Interaction of Type I Receptors of the TGF-β Family with the Immunophilin FKBP-12
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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Cited by
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Metadata
- Authors
- Wang, T., Donahoe, P. K., & Zervos, A. S.
- Venue
- Science
- Published
- 1994-07-29
- Volume
- 265
- Issue
- 5172
- Pages
- 674-676
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1984789406
- Cited by
- 331
- References
- 0
- FWCI
- 12.38
- Type
- journal article
- Language
- en
- Open access
- closed
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- Wang, T., Donahoe, P. K., & Zervos, A. S. (1994). Specific Interaction of Type I Receptors of the TGF-β Family with the Immunophilin FKBP-12. Science. https://doi.org/10.1126/science.7518616
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