Document Type
Article
Publication Date
7-6-2016
Keywords
Post-translational modifications, Stress granules, Stress signalling, Ubiquitin ligases
Digital Object Identifier (DOI)
https://doi.org/10.1038/ncomms12125
Abstract
Stress granules (SGs) harbour translationally stalled messenger ibonucleoproteins 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.
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Citation / Publisher Attribution
Nature Communications, v. 7, art. 12125
Scholar Commons Citation
Jayabalan, Aravinth Kumar; Sanchez, Anthony; Park, Ra Young; Yoon, Sang Pil; Kang, Gum-Yong; Baek, Je-Hyun; Anderson, Paul; Kee, Younghoon; and Ohn, Takbum, "NEDDylation Promotes Stress Granule Assembly" (2016). Molecular Biosciences Faculty Publications. 24.
https://digitalcommons.usf.edu/bcm_facpub/24
