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NEDDylation promotes stress granule assembly

Author

Listed:
  • Aravinth Kumar Jayabalan

    (College of Medicine, Chosun University)

  • Anthony Sanchez

    (Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida)

  • Ra Young Park

    (College of Medicine, Chosun University)

  • Sang Pil Yoon

    (School of Medicine, Jeju National University)

  • Gum-Yong Kang

    (Diatech Korea Co, Ltd)

  • Je-Hyun Baek

    (Diatech Korea Co, Ltd)

  • Paul Anderson

    (Immunology and Allergy, Brigham and Women’s Hospital)

  • Younghoon Kee

    (Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida)

  • Takbum Ohn

    (College of Medicine, Chosun University)

Abstract

Stress granules (SGs) harbour translationally stalled messenger ribonucleoproteins and play important roles in regulating gene expression and cell fate. Here we show that neddylation promotes SG assembly in response to arsenite-induced oxidative stress. Inhibition or depletion of key components of the neddylation machinery concomitantly inhibits stress-induced polysome disassembly and SG assembly. Affinity purification and subsequent mass-spectrometric analysis of Nedd8-conjugated proteins from translationally stalled ribosomal fractions identified ribosomal proteins, translation factors and RNA-binding proteins (RBPs), including SRSF3, a previously known SG regulator. We show that SRSF3 is selectively neddylated at Lys85 in response to arsenite. A non-neddylatable SRSF3 (K85R) mutant do not prevent arsenite-induced polysome disassembly, but fails to support the SG assembly, suggesting that the neddylation pathway plays an important role in SG assembly.

Suggested Citation

  • Aravinth Kumar Jayabalan & Anthony Sanchez & Ra Young Park & Sang Pil Yoon & Gum-Yong Kang & Je-Hyun Baek & Paul Anderson & Younghoon Kee & Takbum Ohn, 2016. "NEDDylation promotes stress granule assembly," Nature Communications, Nature, vol. 7(1), pages 1-14, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12125
    DOI: 10.1038/ncomms12125
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