Members of the Ago (Argonaute) protein family are the mediators of small RNA-guided gene-silencing pathways including RNAi (RNA interference), translational regulation by miRNAs (microRNAs) and transcriptional silencing. Recent findings by Zeng et al. in this issue of the Biochemical Journal demonstrate that Ago proteins are post-translationally modified by phosphorylation of Ser387. Mutating Ser387 to alanine leads to reduced localization of human Ago2 to cytoplasmic P-bodies (processing bodies), cellular sites where RNA turnover and, at least in part, miRNA-guided gene regulation occurs. Zeng et al. further show that a member of the MAPK (mitogen-activated protein kinase) signalling pathway phosphorylates Ago2 at Ser387, suggesting that Ago2-mediated gene silencing might be linked to distinct signalling pathways.
Commentary| July 15 2008
Phosphorylation of Argonaute proteins: regulating gene regulators
Gunter Meister 1
1Center for integrated protein Sciences Munich (CIPSM), Laboratory of RNA Biology, Max–Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
1To whom correspondence should be addressed (email firstname.lastname@example.org).
Search for other works by this author on:
- Views Icon Views
- Share Icon Share
- Cite Icon Cite
Sabine Rüdel, Gunter Meister; Phosphorylation of Argonaute proteins: regulating gene regulators. Biochem J 1 August 2008; 413 (3): e7–e9. doi: https://doi.org/10.1042/BJ20081244
Download citation file: