A redox-mediated conformational change in NQO1 controls binding to microtubules and α-tubulin acetylation

A redox-mediated conformational change in NQO1 controls binding to microtubules and α-tubulin acetylation

The localization of NQO1 near acetylated microtubules has led to the hypothesis that NQO1 may work in concert with the NAD+-dependent deacetylase SIRT2 to regulate acetyl α-tubulin (K40) levels on microtubules. NQO1 catalyzes the oxidation of NADH to NAD+ and may supplement levels of NAD+ near micro...

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Bibliographic Details
Main Authors: David Siegel, Stephanie Bersie, Peter Harris, Andrea Di Francesco, Michael Armstrong, Nichole Reisdorph, Michel Bernier, Rafael de Cabo, Kristofer Fritz, David Ross
Format: Article
Language:English
Published: Elsevier 2021-02-01
Series:Redox Biology
Subjects:
NQO1
SIRT2
α-Tubulin
Acetylation
Pyridine nucleotides
Microtubules
Online Access:http://www.sciencedirect.com/science/article/pii/S2213231720310454

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http://www.sciencedirect.com/science/article/pii/S2213231720310454

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