Evolutionary Aspects of the Unfolded Protein Response.

Humans Animals Endoribonucleases / metabolism Protein Serine-Threonine Kinases Activating Transcription Factor 6 / genetics Saccharomyces cerevisiae / metabolism Unfolded Protein Response Endoplasmic Reticulum Stress eIF-2 Kinase / genetics

Journal

Cold Spring Harbor perspectives in biology
ISSN: 1943-0264
Titre abrégé: Cold Spring Harb Perspect Biol
Pays: United States
ID NLM: 101513680

Informations de publication

Date de publication:
01 12 2022
Historique:
pmc-release: 01 12 2024
pubmed: 9 8 2022
medline: 6 12 2022
entrez: 8 8 2022
Statut: epublish

Résumé

The unfolded protein response (UPR) is activated when unfolded proteins accumulate in the endoplasmic reticulum (ER). The basic mechanism of the UPR in maintaining ER homeostasis has been clarified from yeast to humans. The UPR is triggered by one or more transmembrane proteins in the ER. The number of canonical UPR sensors/transducers has increased during evolution, from one (IRE1) in yeast to three (IRE1, PERK, and ATF6) in invertebrates and five (IRE1α, IRE1β, PERK, ATF6α, and ATF6β) in vertebrates. Here, I initially describe the four major changes that have occurred during evolution: (1) advent of PERK in metazoans; (2) switch in transcription factor downstream of IRE1 in metazoans; (3) switch in regulator of ER chaperone induction in vertebrates; and (4) increase in the number of ATF6-like local factors in vertebrates. I then discuss the causes of the phenotypes of vertebrate knockout animals and refer to regulated IRE1-dependent decay of mRNAs.

Identifiants

DOI: 10.1101/cshperspect.a041262 PMID: 35940910 PMC: PMC9732898
pubmed: 35940910
pii: cshperspect.a041262
doi: 10.1101/cshperspect.a041262
pmc: PMC9732898
pii:
doi:

Substances chimiques

Endoribonucleases EC 3.1.-
Protein Serine-Threonine Kinases EC 2.7.11.1
Activating Transcription Factor 6 0
eIF-2 Kinase EC 2.7.11.1

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

Copyright © 2022 Cold Spring Harbor Laboratory Press; all rights reserved.

Auteurs

Kazutoshi Mori (K)

Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Evolutionary Aspects of the Unfolded Protein Response.
questionsmedicales.fr › Eucaryotes › Animaux › Evolutionary Aspects of the Unfolded Protein Response.
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Esterases › Ribonucléases › Endoribonucleases › Evolutionary Aspects of the Unfolded Protein Response.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Evolutionary Aspects of the Unfolded Protein Response.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Facteurs de transcription à motif basique et à glissière à leucines › Facteurs de transcription ATF › Facteur de transcription ATF-6 › Evolutionary Aspects of the Unfolded Protein Response.
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › Evolutionary Aspects of the Unfolded Protein Response.
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Réponse aux protéines mal repliées › Evolutionary Aspects of the Unfolded Protein Response.
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Stress du réticulum endoplasmique › Evolutionary Aspects of the Unfolded Protein Response.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › eIF-2 Kinase › Evolutionary Aspects of the Unfolded Protein Response.