On the mechanism of calcium-dependent activation of NADPH oxidase 5 (NOX5)

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F19%3A00522047" target="_blank" >RIV/86652036:_____/19:00522047 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/20:00559327
Result on the web
<a href="https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15160" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15160</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/febs.15160" target="_blank" >10.1111/febs.15160</a>

Result language
angličtina
Original language name
On the mechanism of calcium-dependent activation of NADPH oxidase 5 (NOX5)
Original language description
It is now accepted that reactive oxygen species (ROS) are not only dangerous oxidative agents but also chemical mediators of the redox cell signaling and innate immune response. A central role in ROS-controlled production is played by the NADPH oxidases (NOXs), a group of seven membrane-bound enzymes (NOX1-5 and DUOX1-2) whose unique function is to produce ROS. Here, we describe the regulation of NOX5, a widespread family member present in cyanobacteria, protists, plants, fungi, and the animal kingdom. We show that the calmodulin-like regulatory EF-domain of NOX5 is partially unfolded and detached from the rest of the protein in the absence of calcium. In the presence of calcium, the C-terminal lobe of the EF-domain acquires an ordered and more compact structure that enables its binding to the enzyme dehydrogenase (DH) domain. Our spectroscopic and mutagenesis studies further identified a set of conserved aspartate residues in the DH domain that are essential for NOX5 activation. Altogether, our work shows that calcium induces an unfolded-to-folded transition of the EF-domain that promotes direct interaction with a conserved regulatory region, resulting in NOX5 activation.
Czech name
—
Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology

Project
<a href="/en/project/LM2015043" target="_blank" >LM2015043: Czech Infrastructure for Integrative Structural Biology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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