HSP90 protein stabilizes unloaded Argonaute complexes and microscopic P-bodies in human cells

Michael Johnston, Marie-Claude Geoffroy, Andrew Sobala, Ron Hay, Gyorgy Hutvagner

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    109 Citations (Scopus)

    Abstract

    Key components of the miRNA-mediated gene regulation pathway are localized in cytoplasmic processing bodies (P-bodies). Mounting evidence suggests that the presence of microscopic P-bodies are not always required for miRNA-mediated gene regulation. Here we have shown that geldanamycin, a well-characterized HSP90 inhibitor, abolishes P-bodies and significantly reduces Argonaute and GW182 protein levels but does not affect the miRNA level and the efficiency of miRNA-mediated gene repression; however, it significantly impairs siRNA loading and the efficacy of exogenous siRNA. Our data suggests that HSP90 protein chaperones Argonautes before binding RNA and may facilitate efficient loading of small RNA.

    Original languageEnglish
    Pages (from-to)1462-1469
    Number of pages8
    JournalMolecular Biology of the Cell
    Volume21
    Issue number9
    DOIs
    Publication statusPublished - 1 May 2010

    Keywords

    • MEDIATED TRANSLATIONAL REPRESSION
    • MESSENGER-RNA DECAY
    • LET-7 MICRORNA
    • GW/P-BODIES
    • PAZ DOMAIN
    • GW182
    • MIRNA
    • TARGET
    • REQUIRES
    • BINDING

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