Prolyl 4-hydroxylation regulates Argonaute 2 stability

Hank H. Qi, Pat P. Ongusaha, Johanna Myllyharju, Dongmei Cheng, Outi Pakkanen, Yujiang Shi, Sam W. Lee, Junmin Peng and Yang Shi ()
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Hank H. Qi: Harvard Medical School, New Research Building 854, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA
Pat P. Ongusaha: Cutaneous Biology Research Center, Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachusetts 02129, USA
Johanna Myllyharju: Oulu Centre for Cell-Matrix Research, University of Oulu
Dongmei Cheng: Center for Neurodegenerative Disease, School of Medicine, Emory University, Atlanta, Georgia 30322, USA
Outi Pakkanen: Oulu Centre for Cell-Matrix Research, University of Oulu
Yujiang Shi: Diabetes, and Hypertension, Brigham and Women’s Hospital and Harvard Medical School, 221 Longwood Avenue, Boston, Massachusetts 02115, USA
Sam W. Lee: Cutaneous Biology Research Center, Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachusetts 02129, USA
Junmin Peng: Center for Neurodegenerative Disease, School of Medicine, Emory University, Atlanta, Georgia 30322, USA
Yang Shi: Harvard Medical School, New Research Building 854, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA

Nature, 2008, vol. 455, issue 7211, 421-424

Abstract: RNA interference: Argonaute 2 stability Argonaute proteins are a part of a larger RNA interference (RNAi) complex, RISC, in which they mediate cleavage of target mRNAs. In this study, Shi and colleagues show that Ago2 interacts with and is hydroxylated by type I collagen prolyl-4-hydroxylase. When this activity is depleted in human or mouse cells, the level of Ago2 is reduced and siRISC activity mediated by the let-7 miRNA is affected. These results suggest that hydroxylation of Ago2, by affecting its stability, can influence the efficiency of RNAi.

Date: 2008
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DOI: 10.1038/nature07186

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