The Protein Disulfide Isomerase Family: from proteostasis to pathogenesis.
Chaperoning
ER-associated degradation
Oxidative protein folding
PDI
Pathogenesis
Proteostasis
Journal
Biochimica et biophysica acta. General subjects
ISSN: 1872-8006
Titre abrégé: Biochim Biophys Acta Gen Subj
Pays: Netherlands
ID NLM: 101731726
Informations de publication
Date de publication:
02 2020
02 2020
Historique:
received:
30
12
2018
revised:
08
03
2019
accepted:
02
04
2019
pubmed:
16
4
2019
medline:
14
7
2020
entrez:
16
4
2019
Statut:
ppublish
Résumé
In mammalian cells, nearly one-third of proteins are inserted into the endoplasmic reticulum (ER), where they undergo oxidative folding and chaperoning assisted by approximately 20 members of the protein disulfide isomerase family (PDIs). PDIs consist of multiple thioredoxin-like domains and recognize a wide variety of proteins via highly conserved interdomain flexibility. Although PDIs have been studied intensely for almost 50 years, exactly how they maintain protein homeostasis in the ER remains unknown, and is important not only for fundamental biological understanding but also for protein misfolding- and aggregation-related pathophysiology. Herein, we review recent advances in structural biology and biophysical approaches that explore the underlying mechanism by which PDIs fulfil their distinct functions to promote productive protein folding and scavenge misfolded proteins in the ER, the primary factory for efficient production of the secretome.
Identifiants
pubmed: 30986509
pii: S0304-4165(19)30080-7
doi: 10.1016/j.bbagen.2019.04.003
pii:
doi:
Substances chimiques
Disulfides
0
Membrane Glycoproteins
0
Peptides
0
endoplasmic reticulum glycoprotein p72
0
Protein Disulfide-Isomerases
EC 5.3.4.1
TXNDC5 protein, human
EC 5.3.4.1
PDIA3 protein, human
EC 5.3.4.1.
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
129338Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.