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α-Synuclein-mediated inhibition of ATF6 processing into COPII vesicles disrupts UPR signaling in Parkinson's disease.

Abstract：

:The unfolded protein response (UPR) monitors the folding environment within the endoplasmic reticulum (ER). Accumulation of misfolded proteins within the ER activates the UPR resulting in the execution of adaptive or non-adaptive signaling pathways. α-Synuclein (α-syn) whose accumulation and aggregation define the pathobiology of Parkinson's disease (PD) has been shown to inhibit ER-Golgi transit of COPII vesicles. ATF6, a protective branch of the UPR, is processed via COPII mediated ER-Golgi transit following its activation via ER stress. Using cellular PD models together with biochemical reconstitution assays, we showed that α-syn inhibited processing of ATF6 directly through physical interactions and indirectly through restricted incorporation into COPII vesicles. Impaired ATF6 signaling was accompanied by decreased ER-associated degradation (ERAD) function and increased pro-apoptotic signaling. The mechanism by which α-syn inhibits ATF6 signaling expands our understanding of the role ER stress and the UPR play in neurodegenerative diseases such as PD.

journal_name

Neurobiol Dis

journal_title

Neurobiology of disease

authors

Credle JJ,Forcelli PA,Delannoy M,Oaks AW,Permaul E,Berry DL,Duka V,Wills J,Sidhu A

doi

10.1016/j.nbd.2015.02.005

subject

Has Abstract

pub_date

2015-04-01 00:00:00

pages

112-125

eissn

0969-9961

issn

1095-953X

pii

S0969-9961(15)00025-X

journal_volume

76

pub_type

杂志文章

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