The cytoplasmic RNA-induced silencing complex (RISC) contains dsRNA binding 
proteins, including protein kinase RNA activator (PACT), transactivation 
response RNA binding protein (TRBP), and Dicer, that process pre-microRNAs into 
mature microRNAs (miRNAs) that target specific mRNA species for regulation. 
There is increasing evidence for important functional interactions between the 
miRNA and nuclear receptor (NR) signaling networks, with recent data showing 
that estrogen, acting through the estrogen receptor, can modulate initial 
aspects of nuclear miRNA processing. Here, we show that the cytoplasmic RISC 
proteins PACT, TRBP, and Dicer are steroid receptor RNA activator (SRA) binding 
NR coregulators that target steroid-responsive promoters and regulate NR 
activity and downstream gene expression. Furthermore, each of the RISC proteins, 
together with Argonaute 2, associates with SRA and specific pre-microRNAs in 
both the nucleus and cytoplasm, providing evidence for links between NR-mediated 
transcription and some of the factors involved in miRNA processing.