The proteasome-interacting Ecm29 protein disassembles the 26S proteasome in response to oxidative stress.

ABSTRACT: Oxidative stress has been implicated in multiple human neurological and other disorders. Proteasomes are multi-subunit proteases critical for the removal of oxidatively damaged proteins. To understand stress-associated human pathologies, it is important to uncover the molecular events underlying the regulation of proteasomes upon oxidative stress. To this end, we investigated H₂O₂ stress-induced molecular changes of the human 26S proteasome and determined that stress-induced 26S proteasome disassembly is conserved from yeast to human. Moreover, we developed and employed a new proteomic approach, XAP (in vivo cross-linking-assisted affinity purification), coupled with stable isotope labeling with amino acids in cell culture (SILAC)-based quantitative MS, to capt

SUBMITTER: Wang X 

PROVIDER: S-EPMC5625060 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature