| Literature DB >> 8798476 |
M J Charng1, P Kinnunen, J Hawker, T Brand, M D Schneider.
Abstract
The FK506-binding protein, FKBP12, is a putative target of type I receptors for transforming growth factor-beta (TbetaR-I). As the FK506 motif that competes with TbetaR-I for FKBP12 resembles an invariant Leu-Pro dipeptide in TbetaR-I, we replaced Leu193 and Pro194 with Ala, along with mutations across the Gly/Ser box. L193A, P194A, and L193A/P194A do not alter TbetaR-I function; T204D partially activates, independent of ligand; L193A/P194A/T204D was an even more potent constitutive mutation. Association with FKBP12 in a yeast two-hybrid assay was disrupted by P194A, L193A/P194A, and L193A/P194A/T204D, but not L193A or T204D alone. Thus, FKBP12 recognition is dispensable for TGFbeta signaling.Entities:
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Year: 1996 PMID： 8798476 DOI： 10.1074/jbc.271.38.22941
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157