Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Binding Sites
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CHO Cells
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COS Cells
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Cell Line
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Cricetinae
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Glutathione Transferase / metabolism
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Histone Deacetylases / metabolism
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Humans
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Hydroxamic Acids / pharmacology
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Molecular Sequence Data
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Nuclear Proteins / chemistry*
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Nuclear Receptor Interacting Protein 1
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Protein Binding
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Amino Acid
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Transfection
Substances
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Adaptor Proteins, Signal Transducing
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Hydroxamic Acids
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NRIP1 protein, human
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Nuclear Proteins
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Nuclear Receptor Interacting Protein 1
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Recombinant Fusion Proteins
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trichostatin A
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Glutathione Transferase
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Histone Deacetylases