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Nat Commun. 2016 Jul 6;7:12125. doi: 10.1038/ncomms12125.

NEDDylation promotes stress granule assembly.

Author information

1
Department of Cellular &Molecular Medicine, College of Medicine, Chosun University, Gwangju 61452, Republic of Korea.
2
Department of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, Tampa, Florida 33620, USA.
3
Department of Anatomy, School of Medicine, Jeju National University, Jeju-Do 690-756, Republic of Korea.
4
Diatech Korea Co, Ltd, Saemal-ro 5-gil, Songpa-gu, Seoul 05807, Republic of Korea.
5
Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Smith652, One Jimmy Fund Way, Boston, Massachusetts 02115, USA.

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.

PMID:
27381497
PMCID:
PMC4935812
DOI:
10.1038/ncomms12125
[Indexed for MEDLINE]
Free PMC Article

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