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

ABSTRACT: 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. Here, we show that K63-linked ubiquitin chains, known to promote proteasome-independent pathways, accumulate primarily in non-cytosolic compartments during oxidative stress induced by sodium arsenite in mammalian cells. Our subcellular ubiquitin proteomic analyses of non-cytosolic compartments expanded 10-fold the pool of proteins known to be ubiquitinated during arsenite stress (2,046) and reveal

SUBMITTER: Maduka AO 

PROVIDER: S-EPMC11213022 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature