RNA-induced silencing complex (RISC) Proteins PACT, TRBP, and Dicer are SRA binding nuclear receptor coregulators

Andrew Redfern, Shane Colley, Dianne Beveridge, Naoya Ikeda, Michael Epis, Xia Li, C.E. Foulds, Lisa Stuart, Andrew Barker, Victoria Russell, Kerry Ramsay, Simon Kobelke, Esme Hatchell, C.J. Payne, Keith Giles, Adriana Messineo, A. Gatignol, R.B. Lanz, B.W. O'Malley, Peter Leedman

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)6536-6541
JournalProceedings of the National Academy of Sciences of the United States of America
Volume110
Issue number16
DOIs
Publication statusPublished - 2013

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