HSP90 Protein Stabilizes Unloaded Argonaute Complexes and Microscopic P-bodies in Human Cells - Archive ouverte HAL Access content directly
Journal Articles Molecular Biology of the Cell Year : 2010

HSP90 Protein Stabilizes Unloaded Argonaute Complexes and Microscopic P-bodies in Human Cells

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Michael Johnston
  • Function : Author
Marie-Claude Geoffroy
Andrew Sobala
  • Function : Author
Gyorgy Hutvagner
  • Function : Author
  • PersonId : 1086464

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 miRNAmediated 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.
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Dates and versions

hal-03082488 , version 1 (18-10-2022)

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Michael Johnston, Marie-Claude Geoffroy, Andrew Sobala, Ron Hay, Gyorgy Hutvagner. HSP90 Protein Stabilizes Unloaded Argonaute Complexes and Microscopic P-bodies in Human Cells. Molecular Biology of the Cell, 2010, 21 (9), pp.1462-1469. ⟨10.1091/mbc.E09⟩. ⟨hal-03082488⟩

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