Christian Mark, Tullet Jennifer M A, Parker Malcolm G
Institute of Reproductive and Developmental Biology, Faculty of Medicine, Imperial College London, London W12 ONN, United Kingdom.
J Biol Chem. 2004 Apr 9;279(15):15645-51. doi: 10.1074/jbc.M313906200. Epub 2004 Jan 21.
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.
受体相互作用蛋白（RIP）140是一种共抑制因子，可通过LXXLL基序被招募至核受体。我们已鉴定出RIP140中四个不同的自主抑制结构域，称为RD1 - 4，它们在哺乳动物和鸟类中高度保守。N端的RD1在曲古抑菌素A存在的情况下抑制转录，这表明它通过一种不依赖组蛋白脱乙酰基酶（HDAC）的机制发挥作用。RD2的抑制活性取决于羧基末端结合蛋白被招募至两个特定的结合位点。使用特异性抑制剂表明，RD2、RD3和RD4能够根据细胞类型，通过依赖HDAC和不依赖HDAC的机制发挥作用。
