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.
Christian
Mark
M
Institute of Reproductive and Developmental Biology, Faculty of Medicine, Imperial College London, London W12 ONN, United Kingdom. m.parker@imperial.ac.uk
Tullet
Jennifer M A
JM
Parker
Malcolm G
MG
D048868:Adaptor Proteins, Signal Transducing; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D016466:CHO Cells; D019556:COS Cells; D002460:Cell Line; D006224:Cricetinae; D005982:Glutathione Transferase / Q000378:metabolism; D006655:Histone Deacetylases / Q000378:metabolism; D006801:Humans; D006877:Hydroxamic Acids / Q000494:pharmacology; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry*; D000078723:Nuclear Receptor Interacting Protein 1; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014162:Transfection
D048868:Adaptor Proteins, Signal Transducing; D006877:Hydroxamic Acids; C000627127:NRIP1 protein, human; D009687:Nuclear Proteins; D000078723:Nuclear Receptor Interacting Protein 1; D011993:Recombinant Fusion Proteins; C012589:trichostatin A; D005982:Glutathione Transferase; D006655:Histone Deacetylases