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

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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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RNA-Induced Silencing Complex
RNA-Binding Proteins
Cytoplasmic and Nuclear Receptors
MicroRNAs
Transcriptional Activation
Proteins
Estrogen Receptors
Protein Kinases
steroid receptor RNA activator
Carrier Proteins
Estrogens
Cytoplasm
Transcription Factors
Steroids
RNA
Gene Expression
Messenger RNA

Cite this

Redfern, Andrew ; Colley, Shane ; Beveridge, Dianne ; Ikeda, Naoya ; Epis, Michael ; Li, Xia ; Foulds, C.E. ; Stuart, Lisa ; Barker, Andrew ; Russell, Victoria ; Ramsay, Kerry ; Kobelke, Simon ; Hatchell, Esme ; Payne, C.J. ; Giles, Keith ; Messineo, Adriana ; Gatignol, A. ; Lanz, R.B. ; O'Malley, B.W. ; Leedman, Peter. / RNA-induced silencing complex (RISC) Proteins PACT, TRBP, and Dicer are SRA binding nuclear receptor coregulators. In: Proceedings of the National Academy of Sciences of the United States of America. 2013 ; Vol. 110, No. 16. pp. 6536-6541.
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title = "RNA-induced silencing complex (RISC) Proteins PACT, TRBP, and Dicer are SRA binding nuclear receptor coregulators",
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.",
author = "Andrew Redfern and Shane Colley and Dianne Beveridge and Naoya Ikeda and Michael Epis and Xia Li and C.E. Foulds and Lisa Stuart and Andrew Barker and Victoria Russell and Kerry Ramsay and Simon Kobelke and Esme Hatchell and C.J. Payne and Keith Giles and Adriana Messineo and A. Gatignol and R.B. Lanz and B.W. O'Malley and Peter Leedman",
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doi = "10.1073/pnas.1301620110",
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Redfern, A, Colley, S, Beveridge, D, Ikeda, N, Epis, M, Li, X, Foulds, CE, Stuart, L, Barker, A, Russell, V, Ramsay, K, Kobelke, S, Hatchell, E, Payne, CJ, Giles, K, Messineo, A, Gatignol, A, Lanz, RB, O'Malley, BW & Leedman, P 2013, 'RNA-induced silencing complex (RISC) Proteins PACT, TRBP, and Dicer are SRA binding nuclear receptor coregulators' Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 16, pp. 6536-6541. https://doi.org/10.1073/pnas.1301620110

RNA-induced silencing complex (RISC) Proteins PACT, TRBP, and Dicer are SRA binding nuclear receptor coregulators. / Redfern, Andrew; Colley, Shane; Beveridge, Dianne; Ikeda, Naoya; Epis, Michael; Li, Xia; Foulds, C.E.; Stuart, Lisa; Barker, Andrew; Russell, Victoria; Ramsay, Kerry; Kobelke, Simon; Hatchell, Esme; Payne, C.J.; Giles, Keith; Messineo, Adriana; Gatignol, A.; Lanz, R.B.; O'Malley, B.W.; Leedman, Peter.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 110, No. 16, 2013, p. 6536-6541.

Research output: Contribution to journalArticle

TY - JOUR

T1 - RNA-induced silencing complex (RISC) Proteins PACT, TRBP, and Dicer are SRA binding nuclear receptor coregulators

AU - Redfern, Andrew

AU - Colley, Shane

AU - Beveridge, Dianne

AU - Ikeda, Naoya

AU - Epis, Michael

AU - Li, Xia

AU - Foulds, C.E.

AU - Stuart, Lisa

AU - Barker, Andrew

AU - Russell, Victoria

AU - Ramsay, Kerry

AU - Kobelke, Simon

AU - Hatchell, Esme

AU - Payne, C.J.

AU - Giles, Keith

AU - Messineo, Adriana

AU - Gatignol, A.

AU - Lanz, R.B.

AU - O'Malley, B.W.

AU - Leedman, Peter

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

U2 - 10.1073/pnas.1301620110

DO - 10.1073/pnas.1301620110

M3 - Article

VL - 110

SP - 6536

EP - 6541

JO - National Academy of Sciences, Proceedings

JF - National Academy of Sciences, Proceedings

SN - 0027-8424

IS - 16

ER -