Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.30.2 (
endonuclease
)
18,621
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Accumulation of misfolded proteins in the endoplasmic reticulum (ER), defined as ER stress, results in activation of the unfolded protein response (UPR). UPR activation is commonly observed in neurodegenerative diseases. ER stress can trigger unconventional secretion mediated by Golgi reassembly and stacking proteins (GRASP) relocalization in cell lines. Here we study the regulation of
GRASP55
by the UPR upon pharmacological induction of ER stress in primary mouse neurons. We demonstrate that UPR activation induces mRNA and protein expression of
GRASP55
, but not GRASP65, in cortical neurons. UPR activation does not result in relocalization of
GRASP55
. UPR-induced
GRASP55
expression is reduced by inhibition of the PERK pathway of the UPR and abolished by inhibition of the
endonuclease
activity of the UPR transducer IRE1. Expression of the IRE1 target XBP1s in the absence of ER stress is not sufficient to increase
GRASP55
expression. Knockdown of
GRASP55
affects neither induction nor recovery of the UPR. We conclude that the UPR regulates the unconventional secretion factor
GRASP55
via a mechanism that requires the IRE1 and the PERK pathway of the UPR in neurons.
...
PMID:Unconventional secretion factor GRASP55 is increased by pharmacological unfolded protein response inducers in neurons. 3073 86
