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Cited by 991

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity

Gibbings, Derrick J., Ciaudo, Constance, Erhardt, Mathieu, Voinnet, Olivier·2009·Nature Cell Biology
DOI 10.1038/ncb1929
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Abstract

In animals, P-bodies or GW-bodies appear to cause the congregation of proteins involved in microRNA (miRNA)-mediated post-transcriptional silencing. The localization of P-bodies does not overlap with that of known organelles and are thus considered independent of lipid bilayers. Nonetheless, an miRNA effector protein, argonaute 2 (AGO2), was initially identified as membrane-associated, and some miRNAs have been found in secreted vesicles (exosomes) that derive from endo-lysosomal compartments called multivesicular bodies (MVBs). Proteins can be sorted in a ubiquitin-dependent manner into MVBs by three heteromeric subcomplexes, collectively termed ESCRT (endosomal sorting complex required for transport), to be further secreted in exosomes and/or degraded by the lysosome. Here we show that GW-bodies containing GW182 and AGO2, two main components of the RNA-induced silencing complex (RISC), are distinct from P-bodies due to their congregation with endosomes and MVBs. Moreover, miRNAs and miRNA-repressible mRNAs are enriched at these cellular membranes, suggesting that endosomes and/or MVBs are sites of miRNA-loaded RISC (miRISC) accumulation and, possibly, action. We further show that purified exosome-like vesicles secreted by MVBs are considerably enriched in GW182, but not P-body components, AGO2 or miRNA-repressible mRNA. Moreover, cells depleted of some ESCRT components show compromised miRNA-mediated gene silencing and over-accumulate GW182, which associates with ubiquitylated proteins. Therefore, GW182, possibly in association with a fraction of miRNA-loaded AGO2, is sorted into MVBs for secretion and/or lysosomal degradation. We propose that this process promotes continuous assembly or disassembly of membrane-associated miRISCs, which is possibly required for miRNA loading or target recognition and subsequent silencing.

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Metadata

Authors
Gibbings, D. J., Ciaudo, C., Erhardt, M., & Voinnet, O.
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2009-08-16
Volume
11
Issue
9
Pages
1143-1149
ISSN
  • 1465-7392 (ISSN-L)
  • 1476-4679
DOI
10.1038/ncb1929
OpenAlex
W1985175917
Cited by
991
References
5
FWCI
21.72
Type
journal article
Language
en
Open access
closed

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