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Argonaute Utilization for miRNA Silencing Is Determined by Phosphorylation-Dependent Recruitment of LIM-Domain-Containing Proteins.
Bridge, Katherine S; Shah, Kunal M; Li, Yigen; Foxler, Daniel E; Wong, Sybil C K; Miller, Duncan C; Davidson, Kathryn M; Foster, John G; Rose, Ruth; Hodgkinson, Michael R; Ribeiro, Paulo S; Aboobaker, A Aziz; Yashiro, Kenta; Wang, Xiaozhong; Graves, Paul R; Plevin, Michael J; Lagos, Dimitris; Sharp, Tyson V.
Afiliación
  • Bridge KS; Centre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
  • Shah KM; Centre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
  • Li Y; Centre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
  • Foxler DE; Centre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
  • Wong SCK; Centre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
  • Miller DC; Centre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
  • Davidson KM; Centre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
  • Foster JG; Centre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
  • Rose R; School of Biological and Chemical Sciences, Queen Mary University of London, Fogg Building, Mile End Road, London E1 4NS, UK.
  • Hodgkinson MR; Department of Biology, University of York, Heslington, York YO10 5DD, UK.
  • Ribeiro PS; Centre for Tumour Biology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK.
  • Aboobaker AA; Department of Zoology, University of Oxford, The Tinbergen Building, South Parks Road, Oxford OX1 3PS, UK.
  • Yashiro K; Cardiac Regeneration and Therapeutics, Osaka University Graduate School of Medicine, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan.
  • Wang X; Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
  • Graves PR; Department of Radiation Oncology, New York-Presbyterian Brooklyn Methodist Hospital, 506 6th Street, Brooklyn, NY 11215, USA.
  • Plevin MJ; Department of Biology, University of York, Heslington, York YO10 5DD, UK.
  • Lagos D; Centre for Immunology and Infection, Hull York Medical School and Department of Biology, University of York, Heslington, York YO10 5DD, UK.
  • Sharp TV; Centre for Molecular Oncology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK. Electronic address: t.sharp@qmul.ac.uk.
Cell Rep ; 20(1): 173-187, 2017 07 05.
Article en En | MEDLINE | ID: mdl-28683311
ABSTRACT
As core components of the microRNA-induced silencing complex (miRISC), Argonaute (AGO) proteins interact with TNRC6 proteins, recruiting other effectors of translational repression/mRNA destabilization. Here, we show that LIMD1 coordinates the assembly of an AGO-TNRC6 containing miRISC complex by binding both proteins simultaneously at distinct interfaces. Phosphorylation of AGO2 at Ser 387 by Akt3 induces LIMD1 binding, which in turn enables AGO2 to interact with TNRC6A and downstream effector DDX6. Conservation of this serine in AGO1 and 4 indicates this mechanism may be a fundamental requirement for AGO function and miRISC assembly. Upon CRISPR-Cas9-mediated knockout of LIMD1, AGO2 miRNA-silencing function is lost and miRNA silencing becomes dependent on a complex formed by AGO3 and the LIMD1 family member WTIP. The switch to AGO3 utilization occurs due to the presence of a glutamic acid residue (E390) on the interaction interface, which allows AGO3 to bind to LIMD1, AJUBA, and WTIP irrespective of Akt signaling.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Silenciador del Gen / MicroARNs / Péptidos y Proteínas de Señalización Intracelular / Proteínas Argonautas / Proteínas con Dominio LIM Límite: Humans Idioma: En Revista: Cell Rep Año: 2017 Tipo del documento: Article País de afiliación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Silenciador del Gen / MicroARNs / Péptidos y Proteínas de Señalización Intracelular / Proteínas Argonautas / Proteínas con Dominio LIM Límite: Humans Idioma: En Revista: Cell Rep Año: 2017 Tipo del documento: Article País de afiliación: Reino Unido