A redox-mediated conformational change in NQO1 controls binding to microtubules and α-tubulin acetylation.
Acetylation
Microtubules
NQO1
Pyridine nucleotides
SIRT2
α-Tubulin
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
02 2021
02 2021
Historique:
received:
21
09
2020
revised:
30
11
2020
accepted:
01
12
2020
pubmed:
29
12
2020
medline:
22
6
2021
entrez:
28
12
2020
Statut:
ppublish
Résumé
The localization of NQO1 near acetylated microtubules has led to the hypothesis that NQO1 may work in concert with the NAD
Identifiants
pubmed: 33360352
pii: S2213-2317(20)31045-4
doi: 10.1016/j.redox.2020.101840
pmc: PMC7772575
pii:
doi:
Substances chimiques
Tubulin
0
NAD(P)H Dehydrogenase (Quinone)
EC 1.6.5.2
NQO1 protein, human
EC 1.6.5.2
Nqo1 protein, mouse
EC 1.6.5.2
Sirtuin 2
EC 3.5.1.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, N.I.H., Intramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
101840Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK109964
Pays : United States
Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.