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

ABSTRACT: 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 microtubules to aid SIRT2 deacetylase activity. While HDAC6 has been shown to regulate the majority of microtubule acetylation at K⁴⁰, SIRT2 is also known to modulate microtubule acetylation (K⁴⁰) in the perinuclear region. In this study we examined the potential roles NQO1 may play in modulating acetyl α-tubulin levels. Knock-out or knock-down of NQO1 or SIRT2 did not change the levels of acetyl α-tubulin in 16HBE human bronchial epit

SUBMITTER: Siegel D 

PROVIDER: S-EPMC7772575 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature