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

Publication Type:
Journal Article
Citation:
Molecular Biology of the Cell, 2010, 21 (9), pp. 1462 - 1469
Issue Date:
2010-05-01
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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. © 2010 by The American Society for Cell Biology.
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