biostudies-literatureLee DHMinistry of Science ICT and Future PlanningUPCI Core FacilityNational Cancer InstituteNCI NIH HHSNational Research Foundation of Korea1870-1885https://www.ebi.ac.uk/biostudies/studies/S-EPMC6152518biostudies-literatureUnknown14(11)Macroautophagy is induced under various stresses to remove cytotoxic materials, including misfolded proteins and their aggregates. These protein cargoes are collected by specific autophagic receptors such as SQSTM1/p62 (sequestosome 1) and delivered to phagophores for lysosomal degradation. To date, little is known about how cells sense and react to diverse stresses by inducing the activity of SQSTM1. Here, we show that the peroxiredoxin-like redox sensor PARK7/DJ-1 modulates the activity of SQSTM1 and the targeting of ubiquitin (Ub)-conjugated proteins to macroautophagy under oxidative stress caused by TNFSF10/TRAIL (tumor necrosis factor [ligand] superfamily, member 10). In this mechanism, TNFSF10 induces the N-terminal arginylation (Nt-arginylation) of the endoplasmic reticulum (ER)-resAutophagyPARK7 modulates autophagic proteolysis through binding to the N-terminally arginylated form of the molecular chaperone HSPA5.PMC6152518P30CA047904R01 CA140554R01CA140554NRF-2014M39Ab5073938project no. 2012M3A9B6055305R03 CA205267P30 CA047904R03CA2052672017R1A6A3A11032084CAP-16-03-KRIBBNRF-2016R1A2B3011389R03CA212125R03 CA2121252015R1D1A1A01058303Kim DKwon YTKim JLSaito YKim STHeo AJLee JLee YJBartlett DLGuo ZSLee DHJeong SShim SMSong XKim BYOh SCfalsePARK7 modulates autophagic proteolysis through binding to the N-terminally arginylated form of the molecular chaperone HSPA5.Macroautophagy is induced under various stresses to remove cytotoxic materials, including misfolded proteins and their aggregates. These protein cargoes are collected by specific autophagic receptors such as SQSTM1/p62 (sequestosome 1) and delivered to phagophores for lysosomal degradation. To date, little is known about how cells sense and react to diverse stresses by inducing the activity of SQSTM1. Here, we show that the peroxiredoxin-like redox sensor PARK7/DJ-1 modulates the activity of SQSTM1 and the targeting of ubiquitin (Ub)-conjugated proteins to macroautophagy under oxidative stress caused by TNFSF10/TRAIL (tumor necrosis factor [ligand] superfamily, member 10). In this mechanism, TNFSF10 induces the N-terminal arginylation (Nt-arginylation) of the endoplasmic reticulum (ER)-res2018-01-01T00:00:00Z20182026-06-14T03:21:00.87Z2026-06-14T03:09:11.145ZS-EPMC61525182997609010.1080/15548627.2018.1491212