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NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin
Author(s) -
Tirone Fabiana,
Cox Jos A.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.02.047
Subject(s) - calmodulin , superoxide , chemistry , enzyme , biochemistry , nadph oxidase , biophysics , biology
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.