Cargando…
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 (K(40)) levels on microtubules. NQO1 catalyzes the oxidation of NADH to NAD(+) and may supplement levels of NAD(+) ne...
Autores principales: | Siegel, David, Bersie, Stephanie, Harris, Peter, Di Francesco, Andrea, Armstrong, Michael, Reisdorph, Nichole, Bernier, Michel, de Cabo, Rafael, Fritz, Kristofer, Ross, David |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7772575/ https://www.ncbi.nlm.nih.gov/pubmed/33360352 http://dx.doi.org/10.1016/j.redox.2020.101840 |
Ejemplares similares
-
Redox modulation of NQO1
por: Siegel, David, et al.
Publicado: (2018) -
Redox state and the sirtuin deacetylases are major factors that regulate the acetylation status of the stress protein NQO1
por: Siegel, David, et al.
Publicado: (2022) -
The diverse functionality of NQO1 and its roles in redox control
por: Ross, David, et al.
Publicado: (2021) -
Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure
por: Howes, Stuart C., et al.
Publicado: (2014) -
Effects of α-tubulin acetylation on microtubule structure and stability
por: Eshun-Wilson, Lisa, et al.
Publicado: (2019)