Localized K63 Ubiquitin Signaling Is Regulated by VCP/p97 During Oxidative Stress.

Under stress conditions, cells reprogram their molecular machineries to mitigate damage and promote survival. Ubiquitin signaling is globally increased during oxidative stress, controlling protein fate and supporting stress defenses at several subcellular compartments. However, the rules driving subcellular ubiquitin localization to promote concerted response mechanisms remain understudied.

Localized K63 ubiquitin signaling is regulated by VCP/p97 during oxidative stress.

Under stress conditions, cells reprogram their molecular machineries to mitigate damage and promote survival. Ubiquitin signaling is globally increased during oxidative stress, controlling protein fate and supporting stress defenses at several subcellular compartments. However, the rules driving subcellular ubiquitin localization to promote these concerted response mechanisms remain understudied.

Expanding Role of Ubiquitin in Translational Control.

The eukaryotic proteome has to be precisely regulated at multiple levels of gene expression, from transcription, translation, and degradation of RNA and protein to adjust to several cellular conditions. Particularly at the translational level, regulation is controlled by a variety of RNA binding proteins, translation and associated factors, numerous enzymes, and by post-translational modifications (PTM). Ubiquitination, a prominent PTM discovered as the signal for protein degradation, has newly emerged as a modulator of protein synthesis by controlling several processes in translation.

Fatty acid synthase inhibits the GlcNAcase during oxidative stress.

The dynamic post-translational modification linked β--acetylglucosamine (-GlcNAc) regulates thousands of nuclear, cytoplasmic, and mitochondrial proteins. Cellular stress, including oxidative stress, results in increased GlcNAcylation of numerous proteins, and this increase is thought to promote cell survival. The mechanisms by which the GlcNAc transferase (OGT) and the GlcNAcase (OGA), the enzymes that add and remove GlcNAc, respectively, are regulated during oxidative stress to alter GlcNAcylation are not fully characterized.