Characterization of Four Autonomous Repression Domains in the Corepressor Receptor Interacting Protein 140
Copyright policy )Characterization of Four Autonomous Repression Domains in the Corepressor Receptor Interacting Protein 140
Receptor interacting protein (RIP) 140 is a corepressor that can be recruited to nuclear receptors by means of LXXLL motifs. We have characterized four distinct autonomous repression domains in RIP140, termed RD1-4, that are highly conserved in mammals and birds. RD1 at the N terminus represses transcription in the presence of trichostatin A, suggesting that it functions by a histone deacetylase (HDAC)-independent mechanism. The repressive activity of RD2 is dependent upon carboxyl-terminal binding protein recruitment to two specific binding sites. Use of specific inhibitors indicates that RD2, RD3, and RD4 are capable of functioning by HDAC-dependent and HDAC-independent mechanisms, depending upon cell type.
- Imperial College London United Kingdom
Binding Sites, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Amino Acid Motifs, Molecular Sequence Data, Nuclear Proteins, CHO Cells, Hydroxamic Acids, Histone Deacetylases, Cell Line, Nuclear Receptor Interacting Protein 1, Protein Structure, Tertiary, Cricetinae, COS Cells, Animals, Humans, Amino Acid Sequence, Adaptor Proteins, Signal Transducing, Glutathione Transferase, Protein Binding
Binding Sites, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Amino Acid Motifs, Molecular Sequence Data, Nuclear Proteins, CHO Cells, Hydroxamic Acids, Histone Deacetylases, Cell Line, Nuclear Receptor Interacting Protein 1, Protein Structure, Tertiary, Cricetinae, COS Cells, Animals, Humans, Amino Acid Sequence, Adaptor Proteins, Signal Transducing, Glutathione Transferase, Protein Binding
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