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

Johnston, M; Geoffroy, MC; Sobala, A; Hay, R; Hutvagner, G

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

Johnston, M Geoffroy, MC Sobala, A Hay, R Hutvagner, G

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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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Field	Value	Language
dc.contributor.author	Johnston, M	en_US
dc.contributor.author	Geoffroy, MC	en_US
dc.contributor.author	Sobala, A	en_US
dc.contributor.author	Hay, R	en_US
dc.contributor.author	Hutvagner, G https://orcid.org/0000-0002-7231-9446	en_US
dc.date.issued	2010-05-01	en_US
dc.identifier.citation	Molecular Biology of the Cell, 2010, 21 (9), pp. 1462 - 1469	en_US
dc.identifier.issn	1059-1524	en_US
dc.identifier.uri	http://hdl.handle.net/10453/15334
dc.description.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. © 2010 by The American Society for Cell Biology.	en_US
dc.relation.ispartof	Molecular Biology of the Cell	en_US
dc.relation.isbasedon	10.1091/mbc.E09-10-0885	en_US
dc.subject.classification	Developmental Biology	en_US
dc.subject.mesh	Cell Line	en_US
dc.subject.mesh	Cell Line, Tumor	en_US
dc.subject.mesh	Hela Cells	en_US
dc.subject.mesh	Cytoplasmic Granules	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Lactams, Macrocyclic	en_US
dc.subject.mesh	Benzoquinones	en_US
dc.subject.mesh	Luciferases	en_US
dc.subject.mesh	RNA-Binding Proteins	en_US
dc.subject.mesh	Eukaryotic Initiation Factor-2	en_US
dc.subject.mesh	MicroRNAs	en_US
dc.subject.mesh	Autoantigens	en_US
dc.subject.mesh	Microscopy, Fluorescence	en_US
dc.subject.mesh	Blotting, Western	en_US
dc.subject.mesh	Blotting, Northern	en_US
dc.subject.mesh	Transfection	en_US
dc.subject.mesh	Signal Transduction	en_US
dc.subject.mesh	Gene Expression	en_US
dc.subject.mesh	RNA Interference	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	HSP90 Heat-Shock Proteins	en_US
dc.subject.mesh	Argonaute Proteins	en_US
dc.subject.mesh	HeLa Cells	en_US
dc.title	HSP90 protein stabilizes unloaded argonaute complexes and microscopic P-bodies in human cells	en_US
dc.type	Journal Article
utslib.citation.volume	9	en_US
utslib.citation.volume	21	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	0903 Biomedical Engineering	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
dc.location.activity	ISI:000277179600004	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology/School of Biomedical Engineering
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
utslib.copyright.status	open_access
pubs.issue	9	en_US
pubs.publication-status	Published	en_US
pubs.volume	21	en_US

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. © 2010 by The American Society for Cell Biology.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/15334