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Titolo:
Transforming growth factor-beta receptor-associated protein 1 is a Smad4 chaperone
Autore:
Wurthner, JU; Frank, DB; Felici, A; Green, HM; Cao, ZH; Schneider, MD; McNally, JG; Lechleider, RJ; Roberts, AB;
Indirizzi:
NCI, Lab Cell Regulat & Carcinogenesis, NIH, Bethesda, MD 20892 USA NCI Bethesda MD USA 20892 t & Carcinogenesis, NIH, Bethesda, MD 20892 USA NCI, Lab Receptor Biol & Gene Express, NIH, Bethesda, MD 20892 USA NCI Bethesda MD USA 20892 iol & Gene Express, NIH, Bethesda, MD 20892 USA Baylor Coll Med, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 ylor Coll Med, Houston, TX 77030 USA Uniformed Serv Univ Hlth Sci, Dept Pharmacol, Bethesda, MD 20814 USA Uniformed Serv Univ Hlth Sci Bethesda MD USA 20814 Bethesda, MD 20814 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 22, volume: 276, anno: 2001,
pagine: 19495 - 19502
SICI:
0021-9258(20010601)276:22<19495:TGFRP1>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
WD-DOMAIN PROTEIN; SIGNALING PATHWAYS; COMPLEX; FKBP12; FORM; PHOSPHORYLATION; IDENTIFICATION; TRANSCRIPTION; INHIBITION; CONVERGE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Roberts, AB NCI, Lab Cell Regulat & Carcinogenesis, NIH, Bldg 41,Rm C629,41 Lib Dr,MSC5055, Bethesda, MD 20892 USA NCI Bldg 41,Rm C629,41 Lib Dr,MSC 5055 Bethesda MD USA 20892 A
Citazione:
J.U. Wurthner et al., "Transforming growth factor-beta receptor-associated protein 1 is a Smad4 chaperone", J BIOL CHEM, 276(22), 2001, pp. 19495-19502

Abstract

Members of the transforming growth factor-beta (TGF-beta) superfamily signal through unique cell membrane receptor serine-threonine kinases to activate downstream targets. TRAP1 is a previously described 96-kDa cytoplasmic protein shown to bind to TGF-beta receptors and suggested to play a role in TGF-beta signaling. We now fully characterize the binding properties of TRAP1, and show that it associates strongly with inactive heteromeric TGF-betaand activin receptor complexes and is released upon activation of signaling. Moreover, we demonstrate that TRAP1 plays a role in the Smad-mediated signal transduction pathway, interacting with the common mediator, Smad4, in a ligand-dependent fashion. While TRAP1 has only a small stimulatory effecton TGF-beta signaling in functional assays, deletion constructs of TRAP1 inhibit TGF-beta signaling and diminish the interaction of Smad4 with Smad2. These are the first data to identify a specific molecular chaperone for Smad4, suggesting a model in which TRAP1 brings Smad4 into the vicinity of the receptor complex and facilitates its transfer to the receptor-activated Smad proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 04:30:15