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, contains a BRCA C-terminal (BRCT) domain that directly interacts with and co-activates Smad2 ( Shimizu et al . 2001 ). Smad3 also directly interacts with the BRCT domain of BRCA1 and TGF-β/Smad3-modified BRCA1-dependent repair of DNA double strand
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by interacting with several nuclear proteins, such as JunD ( Agarwal et al . 1999 ), NF-κB ( Heppner et al . 2001 ), and Smad3 ( Kaji et al . 2001 ). Recent biochemical studies implicate menin in regulating chromatin modifications by interacting
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State Key Laboratory of Veterinary Biotechnology Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, Heilongjiang, China
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( Yokobori & Nishiyama 2017 ). Menin regulates TGF-beta signaling and TGF-beta-induced gene transcription by interacting with Smad3, a TGF-beta downstream effector ( Kaji et al. 2001 ). Menin directly interacts with Smad3 and inhibit Smad3/4-DNA binding at
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Departments of Urology, Anatomic Pathology, Department of Urology, Department of Clinical Chemistry and Laboratory Medicine, Graduate School of Medical Sciences, Kyushu University, 3‐1‐1 Maidashi, Higashi‐ku, Fukuoka 812‐8582, Japan
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previously been reported that TGF-β and AR signaling mutually promoted their respective signals in PC-3 and LNCaP cells in which AR and TGF-βR2 are overexpressed ( Zhu et al . 2008 ). However, in classical TGF-β-induced pathway activation, Smad3/4 functions
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)-1 and -2-containing complexes and Smad3 (a TGF-β signalling component) to promote transcription of target genes; it restricts Wnt pathway target genes transcription by blocking β-catenin from entering the nucleus; in the cytoplasm, menin binds to Akt
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ARC-NET Research Center, Department of Pathology, Department of Pathology, Technische Universität München, Department of Surgical and Gastroenterological Sciences, University of Verona, Policlinico G.B. Rossi c/o Piastra Odontoiatrica, Piazzale L.A. Scuro, 10, 37134 Verona, Italy
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ARC-NET Research Center, Department of Pathology, Department of Pathology, Technische Universität München, Department of Surgical and Gastroenterological Sciences, University of Verona, Policlinico G.B. Rossi c/o Piastra Odontoiatrica, Piazzale L.A. Scuro, 10, 37134 Verona, Italy
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ARC-NET Research Center, Department of Pathology, Department of Pathology, Technische Universität München, Department of Surgical and Gastroenterological Sciences, University of Verona, Policlinico G.B. Rossi c/o Piastra Odontoiatrica, Piazzale L.A. Scuro, 10, 37134 Verona, Italy
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( Agarwal et al . 1999 , 2003 , Kim et al . 2003 ), and with Smad3 inhibiting transforming growth factor-β (TGF-β) signaling pathway ( Kaji et al . 2001 ). Additional interactions include those with the metastasis suppressor NM23 that is involved in DNA
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change ( Supplementary Table 2 , see section on supplementary data given at the end of this article). STAT3 pY705, SMAD3, RPTOR, PRAS40, pT246, and Annexin VII (ANXA7) were moderately inversely correlated with % tumor size change, and four biomarkers
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Division of Surgery, Istituto Auxologico Italiano, Istituto di Ricovero e Cura a Carattere Scientifico (IRCCS), Milan, Italy
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, as described previously ( Zhang et al. 2017 b ). Antibodies against TGFBR2 (mouse mAb, Cat#: 66636-1-Ig, 1:2000), USP15 (Mouse mAb, Cat#: 67557-1-Ig, 1:5000) and phosphorylated SMAD3 (Rabbit mAb, Cat#: ab52903, 1:5000) were purchased from
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Greater Los Angeles Veterans Administration, Los Angeles, California, USA
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. 2011 ). It is possible that the specificity of a miR to a particular TGF-β ligand isoform or downstream effectors may limit some of these unwanted effects. Of these effectors, Smad2, Smad3 and Smad4 activate downstream transcription, but can be
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) signalling molecule Smad3 can transactivate AR and it has been reported that DHT can suppress the ability of TGFβ to promote apoptosis. Additional data examining the AR-associated protein HIC5 (TGFB1I1) in this interaction highlight a complex interplay