The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Quantitative analysis of Argonaute protein reveals microRNA-dependent localization to stress granules
Open accessAbstract
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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Bartel (2004) · doi:10.1016/s0092-8674(04)00045-5 · Cited by 34,714
Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
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Control of translation and mRNA degradation by miRNAs and siRNAs: Table 1.
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Regulation of mRNA Translation and Stability by microRNAs
Fabian, M. R., Sonenberg, N., & Filipowicz, W. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060308-103103 · Cited by 3,214
LNCcation: lncRNA localization and function
Bridges, M. C., Daulagala, A. C., & Kourtidis, A. (2021) · Journal of Cell Biology · doi:10.1083/jcb.202009045 · Cited by 1,556
Metadata
- Authors
- Leung, A. K. L., Calabrese, J. M., & Sharp, P. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-11-28
- Volume
- 103
- Issue
- 48
- Pages
- 18125-18130
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2033469771
- Cited by
- 393
- References
- 5
- FWCI
- 11.21
- Type
- journal article
- Language
- en
- Open access
- green
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