Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051587 | FEBS Letters | 2007 | 7 Pages |
Abstract
Superoxide generation by NADPH oxidase 5 (NOX5) is regulated by Ca2+ 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 Ca2+-dependent manner, changes its conformation and increases the Ca2+ sensitivity of the N terminus-regulated enzymatic activity. This mechanism represents an additional sophistication in the regulation of superoxide production by NOX5.
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Authors
Fabiana Tirone, Jos A. Cox,