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Prolyl 4-hydroxylation regulates Argonaute 2 stability

Author

Listed:
  • 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)

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.

Suggested Citation

  • Hank H. Qi & Pat P. Ongusaha & Johanna Myllyharju & Dongmei Cheng & Outi Pakkanen & Yujiang Shi & Sam W. Lee & Junmin Peng & Yang Shi, 2008. "Prolyl 4-hydroxylation regulates Argonaute 2 stability," Nature, Nature, vol. 455(7211), pages 421-424, September.
    • Handle: RePEc:nat:nature:v:455:y:2008:i:7211:d:10.1038_nature07186
    DOI: 10.1038/nature07186
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