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

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.

Citation / Publisher Attribution

Nature Communications, v. 7, art. 12125

Additional Files

ncomms12125-s1.pdf (3198 kB)
ncomms12125-s2.xls (182 kB)

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