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http://purl.uniprot.org/citations/16720724http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16720724http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16720724http://www.w3.org/2000/01/rdf-schema#comment"The cytoplasmic immunophilin FKBP12, a 12 kDa FK506-binding protein, has been shown to act as an inhibitor for transforming growth factor-beta (TGF-beta) signaling. FKBP12 binds to the glycine- and serine-rich motif (GS motif) of the TGF-beta 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-beta 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."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.org/dc/terms/identifier"doi:10.1677/jme.1.01966"xsd:string
http://purl.uniprot.org/citations/16720724http://purl.org/dc/terms/identifier"doi:10.1677/jme.1.01966"xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Yamaguchi T."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Yamaguchi T."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Sugino H."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Sugino H."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Kurisaki A."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Kurisaki A."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Minakuchi K."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Minakuchi K."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Yamakawa N."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/author"Yamakawa N."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/name"J. Mol. Endocrinol."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/name"J. Mol. Endocrinol."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/pages"569-579"xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/pages"569-579"xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/title"FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type I receptor."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/title"FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type I receptor."xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/volume"36"xsd:string
http://purl.uniprot.org/citations/16720724http://purl.uniprot.org/core/volume"36"xsd:string