1. p160 Myb-Binding Protein Interacts with Prep1 and Inhibits Its Transcriptional Activity▿ †
- Author
-
Guillermo Menendez, Rebecca A. Keough, Elena Longobardi, Víctor M. Díaz, Angela Bachi, Francesco Blasi, Silvia Mori, Carmelo Ferrai, Díaz, V, Mori, S, Longobardi, E, Menendez, G, Ferrai, C, Keough, R, Bachi, A, and Blasi, F
- Subjects
Transcription, Genetic ,Immunoprecipitation ,Transcription Factor ,Molecular Sequence Data ,Biology ,Mice ,Genetic ,hemic and lymphatic diseases ,Animals ,MYB ,Amino Acid Sequence ,Nuclear protein ,Cell Nucleu ,Transcription factor ,Peptide sequence ,NIH 3T3 Cell ,Molecular Biology ,Nuclear Protein ,Regulation of gene expression ,Cell Nucleus ,Homeodomain Proteins ,Nucleoplasm ,Animal ,Binding protein ,fungi ,Pre-B-Cell Leukemia Transcription Factor 1 ,Nuclear Proteins ,RNA-Binding Proteins ,Homeodomain Protein ,Cell Biology ,Articles ,Molecular biology ,DNA-Binding Proteins ,Gene Expression Regulation ,NIH 3T3 Cells ,Carrier Protein ,Carrier Proteins ,Sequence Alignment ,Transcription Factors - Abstract
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 pi 60, 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. Copyright © 2007, American Society for Microbiology. All Rights Reserved.
- Published
- 2007