The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Phosphorylation of Argonaute 2 at serine-387 facilitates its localization to processing bodies
Abstract
Ago (Argonaute) proteins are essential effectors of RNA-mediated gene silencing. To explore potential regulatory mechanisms for Ago proteins, we examined the phosphorylation of human Ago2. We identified serine-387 as the major Ago2 phosphorylation site in vivo. Phosphorylation of Ago2 at serine-387 was significantly induced by treatment with sodium arsenite or anisomycin, and arsenite-induced phosphorylation was inhibited by a p38 MAPK (mitogen-activated protein kinase) inhibitor, but not by inhibitors of JNK (c-Jun N-terminal kinase) or MEK [MAPK/ERK (extracellular-signal-regulated kinase) kinase]. MAPKAPK2 (MAPK-activated protein kinase-2) phosphorylated bacterially expressed full-length human Ago2 at serine-387 in vitro, but not the S387A mutant. Finally, mutation of serine-387 to an alanine residue or treatment of cells with a p38 MAPK inhibitor reduced the localization of Ago2 to processing bodies. These results suggest a potential regulatory mechanism for RNA silencing acting through Ago2 serine-387 phosphorylation mediated by the p38 MAPK pathway.
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Metadata
- Authors
- Zeng, Y., Sankala, H., Zhang, X., & Graves, P. R.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2008-07-15
- Volume
- 413
- Issue
- 3
- Pages
- 429-436
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2161751301
- Cited by
- 225
- References
- 9
- FWCI
- 6.58
- Type
- journal article
- Language
- en
- Open access
- closed
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- Zeng, Y., Sankala, H., Zhang, X., & Graves, P. R. (2008). Phosphorylation of Argonaute 2 at serine-387 facilitates its localization to processing bodies. Biochemical Journal. https://doi.org/10.1042/bj20080599
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