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• W2033469771 abstract "Argonaute proteins associate with microRNAs (miRNAs) that bind mRNAs through partial base-pairings to primarily repress translation in animals. A fraction of Argonaute proteins and miRNAs biochemically cosediment with polyribosomes, yet another fraction paradoxically accumulates in ribosome-free processing bodies (PBs) in the cytoplasm. In this report, we give a quantitative account of the Argonaute protein localization and dynamics in living cells in different cellular states. We find that the majority of Argonaute is distributed diffusely in the cytoplasm, and, when cells are subjected to stress, Argonaute proteins accumulate to newly assembled structures known as stress granules (SGs) in addition to PBs. Argonaute proteins displayed distinct kinetics at different structures: exchange faster at SGs and much slower at PBs. Further, miRNAs are required for the Argonaute protein localization to SGs but not PBs. These quantitative kinetic data provide insights into miRNA-mediated repression." @default.
• W2033469771 created "2016-06-24" @default.
• W2033469771 creator A5021874905 @default.
• W2033469771 creator A5022945869 @default.
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• W2033469771 date "2006-11-28" @default.
• W2033469771 modified "2023-10-05" @default.
• W2033469771 title "Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules" @default.
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• W2033469771 doi "https://doi.org/10.1073/pnas.0608845103" @default.
• W2033469771 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1838717" @default.
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