ArticleAutophagy2018
PARK7 modulates autophagic proteolysis through binding to the N-terminally arginylated form of the molecular chaperone HSPA5.
Article in Autophagy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Impairment of Macrophage Functions by the Senescence-Associated Secretory Phenotype of Vascular Smooth Muscle Cells-Brief Report.Arteriosclerosis, thrombosis, and vascular biology · 2026Article
- Viral infection and brain inflammation with seizures in PARK7 deficiency.Journal of human immunity · 2026Article
- Article
- Exploration of key genes associated with oxidative stress in polycystic ovary syndrome and experimental validation.Frontiers in medicine · 2025Article
- Mechanistic insight of neurodegeneration due to micro/nano-plastic-induced gut dysbiosis.Archives of toxicology · 2025Review
- Obesity and Environmental Risk Factors Significantly Modify the Association between Ischemic Stroke and the Hero ChaperoneLife (Basel, Switzerland) · 2024Article
- Chronic noise exposure induces Alzheimer's disease-like neuropathology and cognitive impairment via ferroptosis in rat hippocampus.Environmental health and preventive medicine · 2024Article
- DJ-1-mediated p62 degradation delays intervertebral disc degeneration by inhibiting apoptosis of nucleus pulposus cells.Apoptosis : an international journal on programmed cell death · 2023Article
- The novel circular RNA CircMef2c is positively associated with muscle growth in Nile tilapia.Genomics · 2023Article
- Monitoring the Activation of Selective Autophagy via N-Terminal Arginylation.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Ubr1-induced selective endophagy/autophagy protects against the endosomal and CaCellular and molecular life sciences : CMLS · 2022Article
- Disuse-associated loss of the protease LONP1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength.Nature communications · 2022Article
- Crosstalk between HSPA5 arginylation and sequential ubiquitination leads to AKT degradation through autophagy flux.Autophagy · 2021Article
- Mitochondrial LonP1 protease is implicated in the degradation of unstable Parkinson's disease-associated DJ-1/PARK 7 missense mutants.Scientific reports · 2021Article
- PARK7 maintains the stemness of glioblastoma stem cells by stabilizing epidermal growth factor receptor variant III.Oncogene · 2021Article
- The Cross-Links of Endoplasmic Reticulum Stress, Autophagy, and Neurodegeneration in Parkinson's Disease.Frontiers in aging neuroscience · 2021Review
- Phenotypic Characteristics and Copy Number Variants in a Cohort of Colombian Patients with VACTERL Association.Molecular syndromology · 2020Article
- Review
- DJ-1 Regulates Microglial Polarization Through P62-Mediated TRAF6/IRF5 Signaling in Cerebral Ischemia-Reperfusion.Frontiers in cell and developmental biology · 2020Article
Corrections and comments
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Authors and funding
16 authors at 6 institutions in 5 countries.
Funding
Abstract
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)-residing molecular chaperone HSPA5/BiP/GRP78, leading to cytosolic accumulation of Nt-arginylated HSPA5 (R-HSPA5). In parallel, TNFSF10 induces the oxidation of PARK7. Oxidized PARK7 acts as a co-chaperone-like protein that binds the ER-derived chaperone R-HSPA5, a member of the HSPA/HSP70 family. By forming a complex with PARK7 (and possibly misfolded protein cargoes), R-HSPA5 binds SQSTM1 through its Nt-Arg, facilitating self-polymerization of SQSTM1 and the targeting of SQSTM1-cargo complexes to phagophores. The 3-way interaction among PARK7, R-HSPA5, and SQSTM1 is stabilized by the Nt-Arg residue of R-HSPA5. PARK7-deficient cells are impaired in the targeting of R-HSPA5 and SQSTM1 to phagophores and the removal of Ub-conjugated cargoes. Our results suggest that PARK7 functions as a co-chaperone for R-HSPA5 to modulate autophagic removal of misfolded protein cargoes generated by oxidative stress.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.