Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules
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No Canadian affiliation. An affiliation-only frame — the usual design — would never have seen this work. It is one of the works that make the case for inverting the frame.
Machine scores (provisional)
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- Teacher spread
- 0.297 · how far apart the two teachers sit on this one work
- Validation status
score_only:v0-immature-baseline· verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it
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.
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The record
- Venue
- Proceedings of the National Academy of Sciences
- Topic
- RNA Research and Splicing
- Field
- Biochemistry, Genetics and Molecular Biology
- Canadian institutions
- —
- Funders
- McGill UniversityUniversity of PennsylvaniaUniversity of AlbertaUniversity of DundeeNational Cancer InstituteNational Science Foundation
- Keywords
- ArgonauteBiologyCell biologymicroRNACytoplasmTranslation (biology)PolysomeRibosomeRNARNA interferenceMessenger RNAGeneticsGene
- Has abstract in OpenAlex
- yes