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Rebecca A Keough - One of the best experts on this subject based on the ideXlab platform.
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ribosomal stress induces processing of mybbp1a and its translocation from the nucleolus to the nucleoplasm
Genes to Cells, 2007Co-Authors: Tomohiro Yamauchi, Rebecca A Keough, Thomas J Gonda, Shunsuke IshiiAbstract:Myb-binding Protein 1a (Mybbp1a) was originally identified as a c-myb proto-oncogene product (c-Myb)-interacting Protein, and also binds to various other transcription factors. The 160-kDa Mybbp1a Protein (P160) is ubiquitously expressed and is post-translationally processed in some types of cells to generate an amino-terminal 67 kDa fragment (p67). Despite its interaction with various transcription factors, Mybbp1a is localized predominantly, but not exclusively, in nucleoli. Here, we have purified the two Mybbp1a-containing complexes. The smaller complex contained p67 and p140, which lacked the C-terminal region of P160 containing the nucleolar localization sequences. The larger complex contained the intact P160 and various ribosomal subunits. Treatment of cells with actinomycin D (ActD), cisplatin or UV, all of which inhibit ribosome biogenesis, induced processing of P160 into p140 and p67. ActD, cisplatin and UV also induced a translocation of Mybbp1a from the nucleolus to the nucleoplasm. Both small and large Mybbp1a complexes contained nucleophosmin and nucleolin. In contrast, nucleostemin was detected only in the large complex, while the cell cycle-regulated Protein EBP1 was only in the small complex. These results suggest that Mybbp1a may connect the ribosome biogenesis and the Myb-dependent transcription, which controls cell cycle progression and proliferation. © 2008 The Authors Journal compilation
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P160 myb binding Protein interacts with prep1 and inhibits its transcriptional activity
Molecular and Cellular Biology, 2007Co-Authors: Victor M Diaz, Elena Longobardi, Silvia Mori, Guillermo Menendez, Carmelo Ferrai, Rebecca A Keough, Angela Bachi, Francesco BlasiAbstract:Prep1 is known to interact in vivo with Pbx1 to regulate development and organogenesis. We have identified a novel Prep1-interacting Protein, P160 c-Myb binding Protein (P160). P160 and Pbx1 compete for Prep1 in vitro, and P160 inhibits Prep1-dependent HoxB2 expression in retinoic acid-treated NT2-D1 cells. The N-terminal physiologically truncated form of P160, p67, binds the sequence 63LFPLL67 in the HR1 domain of Prep1. Mutation of both L63 and L66 impairs the binding of Prep1 to both P160/p67 and Pbx1. The sequences required to bind Prep1 are mainly located in residues 51 to 151. Immunofluorescence colocalization and coimmunoprecipitation of endogenous P160 and Prep1 are induced by ActD, which translocates P160 from the nucleolus to the nucleoplasm. These data therefore show that P160 is a novel regulator of Prep1-Pbx1 transcriptional activity.
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molecular cloning and chromosomal mapping of the human homologue of myb binding Protein P160 1a mybbp1a to 17p13 3
Genomics, 1999Co-Authors: Rebecca A Keough, Erica Woollatt, Joanna Crawford, Grant R Sutherland, Sarah J Plummer, Graham Casey, Thomas J GondaAbstract:We have previously isolated and characterized murine MYB binding Protein (P160) 1a, a Protein that specifically interacts with the leucine zipper motif within the negative regulatory domain of the c-Myb proto-oncoProtein. We now describe the molecular cloning of the human MYBBP1A cDNA and chromosomal localization to 17p13.3 by fluorescence in situ hybridization analysis. Given the likely presence of a tumor suppressor gene (or genes) within this region of chromosome 17, the position of MYBBP1A was further mapped by radiation hybrid analysis and was found to lie between markers D17S1828 and D17S938. A P1 artificial chromosome clone containing the 5' region of MYBBP1A was isolated and indicates a physical linkage between MYBBP1A and the 15-lipoxygenase gene (ALOX15). A novel, polymorphic (CA)(25) dinucleotide repeat was also isolated from this PAC and may serve as a useful marker for MYBBP1A and this region of chromosome 17.
Francesco Blasi - One of the best experts on this subject based on the ideXlab platform.
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P160 myb binding Protein interacts with prep1 and inhibits its transcriptional activity
Molecular and Cellular Biology, 2007Co-Authors: Victor M Diaz, Elena Longobardi, Silvia Mori, Guillermo Menendez, Carmelo Ferrai, Rebecca A Keough, Angela Bachi, Francesco BlasiAbstract:Prep1 is known to interact in vivo with Pbx1 to regulate development and organogenesis. We have identified a novel Prep1-interacting Protein, P160 c-Myb binding Protein (P160). P160 and Pbx1 compete for Prep1 in vitro, and P160 inhibits Prep1-dependent HoxB2 expression in retinoic acid-treated NT2-D1 cells. The N-terminal physiologically truncated form of P160, p67, binds the sequence 63LFPLL67 in the HR1 domain of Prep1. Mutation of both L63 and L66 impairs the binding of Prep1 to both P160/p67 and Pbx1. The sequences required to bind Prep1 are mainly located in residues 51 to 151. Immunofluorescence colocalization and coimmunoprecipitation of endogenous P160 and Prep1 are induced by ActD, which translocates P160 from the nucleolus to the nucleoplasm. These data therefore show that P160 is a novel regulator of Prep1-Pbx1 transcriptional activity.
Victor M Diaz - One of the best experts on this subject based on the ideXlab platform.
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P160 myb binding Protein interacts with prep1 and inhibits its transcriptional activity
Molecular and Cellular Biology, 2007Co-Authors: Victor M Diaz, Elena Longobardi, Silvia Mori, Guillermo Menendez, Carmelo Ferrai, Rebecca A Keough, Angela Bachi, Francesco BlasiAbstract:Prep1 is known to interact in vivo with Pbx1 to regulate development and organogenesis. We have identified a novel Prep1-interacting Protein, P160 c-Myb binding Protein (P160). P160 and Pbx1 compete for Prep1 in vitro, and P160 inhibits Prep1-dependent HoxB2 expression in retinoic acid-treated NT2-D1 cells. The N-terminal physiologically truncated form of P160, p67, binds the sequence 63LFPLL67 in the HR1 domain of Prep1. Mutation of both L63 and L66 impairs the binding of Prep1 to both P160/p67 and Pbx1. The sequences required to bind Prep1 are mainly located in residues 51 to 151. Immunofluorescence colocalization and coimmunoprecipitation of endogenous P160 and Prep1 are induced by ActD, which translocates P160 from the nucleolus to the nucleoplasm. These data therefore show that P160 is a novel regulator of Prep1-Pbx1 transcriptional activity.
Yuzuru Shiio - One of the best experts on this subject based on the ideXlab platform.
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quantitative proteomics identifies the myb binding Protein P160 as a novel target of the von hippel lindau tumor suppressor
PLOS ONE, 2011Co-Authors: Yanlai Lai, Mei Qiao, Meihua Song, Susan T Weintraub, Yuzuru ShiioAbstract:Background The von Hippel-Lindau (VHL) tumor suppressor gene encodes a component of a ubiquitin ligase complex, which is best understood as a negative regulator of hypoxia inducible factor (HIF). VHL ubiquitinates and degrades the α subunits of HIF, and this is proposed to suppress tumorigenesis and tumor angiogenesis. However, several lines of evidence suggest that there are unidentified substrates or targets for VHL that play important roles in tumor suppression.
Angela Bachi - One of the best experts on this subject based on the ideXlab platform.
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P160 myb binding Protein interacts with prep1 and inhibits its transcriptional activity
Molecular and Cellular Biology, 2007Co-Authors: Victor M Diaz, Elena Longobardi, Silvia Mori, Guillermo Menendez, Carmelo Ferrai, Rebecca A Keough, Angela Bachi, Francesco BlasiAbstract:Prep1 is known to interact in vivo with Pbx1 to regulate development and organogenesis. We have identified a novel Prep1-interacting Protein, P160 c-Myb binding Protein (P160). P160 and Pbx1 compete for Prep1 in vitro, and P160 inhibits Prep1-dependent HoxB2 expression in retinoic acid-treated NT2-D1 cells. The N-terminal physiologically truncated form of P160, p67, binds the sequence 63LFPLL67 in the HR1 domain of Prep1. Mutation of both L63 and L66 impairs the binding of Prep1 to both P160/p67 and Pbx1. The sequences required to bind Prep1 are mainly located in residues 51 to 151. Immunofluorescence colocalization and coimmunoprecipitation of endogenous P160 and Prep1 are induced by ActD, which translocates P160 from the nucleolus to the nucleoplasm. These data therefore show that P160 is a novel regulator of Prep1-Pbx1 transcriptional activity.
