Endoplasmic reticulum stress differentially inhibits endoplasmic reticulum and inner nuclear membrane protein quality control degradation pathways.
Animals
Cattle
Cell Nucleus
/ metabolism
Endoplasmic Reticulum
/ metabolism
Endoplasmic Reticulum Stress
Gene Expression Regulation, Fungal
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
/ chemistry
Membrane Proteins
/ metabolism
Membrane Transport Proteins
/ metabolism
Metalloendopeptidases
/ metabolism
Nuclear Envelope
/ metabolism
Phosphoric Monoester Hydrolases
/ metabolism
Plasmids
/ metabolism
Protein Transport
Protein Unfolding
Proteolysis
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ metabolism
Ubiquitin-Protein Ligases
/ metabolism
E3 ubiquitin ligase
Saccharomyces cerevisiae
Ste24
endoplasmic reticulum stress (ER stress)
endoplasmic reticulum–associated protein degradation (ERAD)
inner nuclear membrane-associated degradation (INMAD)
protein quality control
protein translocation
translocon
yeast genetics
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
20 12 2019
20 12 2019
Historique:
received:
22
07
2019
revised:
04
11
2019
pubmed:
15
11
2019
medline:
23
6
2020
entrez:
15
11
2019
Statut:
ppublish
Résumé
Endoplasmic reticulum (ER) stress occurs when the abundance of unfolded proteins in the ER exceeds the capacity of the folding machinery. Despite the expanding cadre of characterized cellular adaptations to ER stress, knowledge of the effects of ER stress on cellular physiology remains incomplete. We investigated the impact of ER stress on ER and inner nuclear membrane protein quality control mechanisms in
Identifiants
pubmed: 31723032
pii: S0021-9258(20)30290-8
doi: 10.1074/jbc.RA119.010295
pmc: PMC6926463
doi:
Substances chimiques
Membrane Proteins
0
Membrane Transport Proteins
0
SEC62 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
HRD1 protein, S cerevisiae
EC 2.3.2.27
Rkr1 protein, S cerevisiae
EC 2.3.2.27
SSM4 protein, S cerevisiae
EC 2.3.2.27
Ubiquitin-Protein Ligases
EC 2.3.2.27
Phosphoric Monoester Hydrolases
EC 3.1.3.2
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
EC 3.2.1.96
Metalloendopeptidases
EC 3.4.24.-
STE24 protein, S cerevisiae
EC 3.4.24.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
19814-19830Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM046904
Pays : United States
Organisme : NIGMS NIH HHS
ID : R15 GM111713
Pays : United States
Organisme : NIGMS NIH HHS
ID : R37 GM046904
Pays : United States
Informations de copyright
© 2019 Buchanan et al.
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