| The mouse homologue of the human receptor interacting protein 140 ( RIP 140 ) was isolated from a mouse embryonic cDNA library in yeast two hybrid screening experiments by using the ligand binding domain ( LBD ) of nuclear orphan receptor TR 2 as the bait . ^^^ Cloning and characterization of mouse RIP 140 , a corepressor for nuclear orphan receptor TR 2 . ^^^ The receptor interacting domains of mouse RIP 140 were mapped to the regions containing the LXXLL motif ( where L is leucine and 10 is any amino acid ) , and the RIP 140 interacting domain of TR 2 was mapped to its C terminal 10 to 20 amino acid sequence , a putative activation function 2 ( AF 2 ) region . ^^^ In a GAL 4 reporter system and a reporter driven by the proximal region of the TR 2 promoter , RIP 140 functioned as a corepressor for both a GAL 4 DNA binding domain ( BD ) TR 2 fusion and the wild type receptor . ^^^ Finally , it was demonstrated that in the presence of RIP 140 , a cytosolic , green fluorescent protein tagged TR 2 LBD translocated into the nucleus , and TR 2 and RIP 140 were coimmunoprecipitated from the cell extract , indicating that the interaction between RIP 140 and the LBD of TR 2 occurred in vivo . ^^^ |