Revealing functional insights into ER proteostasis through proteomics and interactomics.
Animals
Endoplasmic Reticulum
/ metabolism
Endoplasmic Reticulum Stress
/ physiology
Humans
Membrane Proteins
/ chemistry
Molecular Chaperones
/ chemistry
Protein Binding
Protein Folding
Protein Interaction Maps
/ physiology
Proteome
/ analysis
Proteomics
/ methods
Proteostasis
/ physiology
Unfolded Protein Response
/ physiology
Affinity purification-mass spectrometry
Endoplasmic reticulum
Mass spectrometry
Protein quality control
Unfolded protein response
Journal
Experimental cell research
ISSN: 1090-2422
Titre abrégé: Exp Cell Res
Pays: United States
ID NLM: 0373226
Informations de publication
Date de publication:
01 02 2021
01 02 2021
Historique:
received:
31
08
2020
revised:
23
11
2020
accepted:
28
11
2020
pubmed:
11
12
2020
medline:
16
6
2021
entrez:
10
12
2020
Statut:
ppublish
Résumé
The endoplasmic reticulum (ER), responsible for processing approximately one-third of the human proteome including most secreted and membrane proteins, plays a pivotal role in protein homeostasis (proteostasis). Dysregulation of ER proteostasis has been implicated in a number of disease states. As such, continued efforts are directed at elucidating mechanisms of ER protein quality control which are mediated by transient and dynamic protein-protein interactions with molecular chaperones, co-chaperones, protein folding and trafficking factors that take place in and around the ER. Technological advances in mass spectrometry have played a pivotal role in characterizing and understanding these protein-protein interactions that dictate protein quality control mechanisms. Here, we highlight the recent progress from mass spectrometry-based investigation of ER protein quality control in revealing the topological arrangement of the proteostasis network, stress response mechanisms that adjust the ER proteostasis capacity, and disease specific changes in proteostasis network engagement. We close by providing a brief outlook on underexplored areas of ER proteostasis where mass spectrometry is a tool uniquely primed to further expand our understanding of the regulation and coordination of protein quality control processes in diverse diseases.
Identifiants
pubmed: 33301765
pii: S0014-4827(20)30670-4
doi: 10.1016/j.yexcr.2020.112417
pmc: PMC8128161
mid: NIHMS1659027
pii:
doi:
Substances chimiques
Membrane Proteins
0
Molecular Chaperones
0
Proteome
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
112417Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM133552
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM065086
Pays : United States
Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
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