Display Settings:


Send to:

Choose Destination
See comment in PubMed Commons below
FEBS Lett. 2007 Mar 20;581(6):1202-8. Epub 2007 Mar 1.

NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin.

Author information

  • 1Department of Biochemistry, University of Geneva, Geneva 4, Switzerland.


Superoxide generation by NADPH oxidase 5 (NOX5) is regulated by Ca(2+) through intramolecular activation of the C-terminal catalytic domain by the EF-hand-containing N-terminal regulatory domain. The C terminus contains a consensus calmodulin-binding domain (CaMBD), which, however, is not the binding site of the N-terminal regulatory domain. Here we show by pull down, cross-linking, fluorimetry and by enzymatic assays, that calmodulin binds to this CaMBD in a Ca(2+)-dependent manner, changes its conformation and increases the Ca(2+) sensitivity of the N terminus-regulated enzymatic activity. This mechanism represents an additional sophistication in the regulation of superoxide production by NOX5.

[PubMed - indexed for MEDLINE]
Free full text

LinkOut - more resources

Full Text Sources

Other Literature Sources

Molecular Biology Databases

PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk