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Science 29 July 1994:
Vol. 265. no. 5172, pp. 674 - 676
DOI: 10.1126/science.7518616
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Articles

Science, Vol 265, Issue 5172, 674-676
Copyright © 1994 by American Association for the Advancement of Science

articles

Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12

T Wang, PK Donahoe, and AS Zervos

Cutaneous Biology Research Center, Massachusetts General Hospital, Boston, MA 02114.

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.


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