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DJ-1 modulates the unfolded protein response and cell death via upregulation of ATF4 following ER stress.

Abstract：

:The unfolded protein response (UPR) triggered by endoplasmic reticulum (ER) stress is a feature of many neurodegenerative diseases including Alzheimer's disease, Huntington's disease and Parkinson's disease (PD). Although the vast majority of PD is sporadic, mutations in a number of genes including PARK7 which encodes the protein DJ-1 have been linked to early-onset, familial PD. In this regard, both PD of sporadic and genetic origins exhibit markers of ER stress-induced UPR. However, the relationship between pathogenic mutations in PARK7 and ER stress-induced UPR in PD pathogenesis remains unclear. In most contexts, DJ-1 has been shown to protect against neuronal injury. However, we find that DJ-1 deficiency ameliorates death in the context of acute ER stress in vitro and in vivo. DJ-1 loss decreases protein and transcript levels of ATF4, a transcription factor critical to the ER response and reduces the levels of CHOP and BiP, its downstream effectors. The converse is observed with DJ-1 over-expression. Importantly, we find that over-expression of wild-type and PD-associated mutant form of PARK7L166P, enhances ER stress-induced neuronal death by regulating ATF4 transcription and translation. Our results demonstrate a previously unreported role for wild-type and mutant DJ-1 in the regulation of UPR and provides a potential link to PD pathogenesis.

journal_name

Cell Death Dis

journal_title

Cell death & disease

authors

Yang J,Kim KS,Iyirhiaro GO,Marcogliese PC,Callaghan SM,Qu D,Kim WJ,Slack RS,Park DS

doi

10.1038/s41419-019-1354-2

subject

Has Abstract

pub_date

2019-02-12 00:00:00

pages

135

issue

2

issn

2041-4889

pii

10.1038/s41419-019-1354-2

journal_volume

10

pub_type

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