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- W2125546633 abstract "The cytoplasmic immunophilin FKBP12, a 12 kDa FK506-binding protein, has been shown to act as an inhibitor for transforming growth factor-β (TGF-β) signaling. FKBP12 binds to the glycine- and serine-rich motif (GS motif) of the TGF-β type I receptor, and functions as a secure switch to prevent the leaky signal. Upon stimulation with ligand, FKBP12 is released from the receptor to fully propagate the signal. We found that activin, a member of TGF-β superfamily, also induced the dissociation of FKBP12 from the activin type I receptor (ALK4). However, we observed that the released FKBP12 associates again with the receptor a few hours later. FKBP12 also interacted with another inhibitory molecule of activin signal, Smad7, in an activin-dependent manner, and formed a complex with Smad7 on the type I receptor. FK506, a chemical ligand for FKBP12, which dissociates FKBP12 from the receptor, decreased the interaction between Smad7 and Smad ubiquitin regulatory factor 1 (Smurf1). FK506 also inhibited the ubiquitination of the type I receptor by Smurf1. These findings indicate a new inhibitory function of FKBP12 as an adaptor molecule for the Smad7–Smurf1 complex to regulate the duration of the activin signal." @default.
- W2125546633 created "2016-06-24" @default.
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- W2125546633 date "2006-06-01" @default.
- W2125546633 modified "2023-10-12" @default.
- W2125546633 title "FKBP12 functions as an adaptor of the Smad7–Smurf1 complex on activin type I receptor" @default.
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- W2125546633 doi "https://doi.org/10.1677/jme.1.01966" @default.
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