FKBP12 is not required for the modulation of transforming growth factor β receptor I signaling activity in embryonic fibroblasts and thymocytes

Craig H. Bassing, Weinian Shou, Scott Muir, Joseph Heitman, Martin M. Matzuk, Xiao Fan Wang

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26 Scopus citations


Transforming growth factor β (TGF-β) signals through a heteromeric complex of type I and type II transmembrane serine-threonine kinases. Recent evidence suggests that the immunophilin FKBP12 modulates the activity of the type I receptor, based on data that immunosuppressive drugs that disrupt FKBP12 binding to the type I receptor enhance TGF-β signaling in mink lung epithelial cells, and overexpression of FKBP12 inhibits type I receptor phosphorylation by the type II receptor. To determine the physiological relevance of the FKBP12-TGF-β receptor I interaction, we investigated whether disruption of this interaction affects TGF-β-signaling in primary mouse embryo fibroblasts and thymocytes. We found that the addition of excess drugs had no effect on either TGF-β-mediated transcriptional responses or growth inhibition. Dose-response curves for TGF-β-mediated signaling in primary fibroblasts and thymocytes isolated from either wild-type or FKBP12- deficient mice were identical. Taken together, our results indicate that FKBP12 does not play a unique physiological role in TGF-β signaling in primary fibroblasts and thymocytes.

Original languageEnglish (US)
Pages (from-to)223-228
Number of pages6
JournalCell Growth and Differentiation
Issue number3
StatePublished - Aug 11 1998


ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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