Mechanisms of activation of NADPH oxidases

Robert A. Clark, Terry Kay Epperson, Anthony J. Valente

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14 Scopus citations

Abstract

The member of the NOX family of enzymes are expressed in a variety of tissues and serve a number of functions. There is a high level of conservation of primary protein sequence, as well as functional features, although specialized responses are beginning to emerge. In this context, our data demonstrate that the NOX1 cytoplasmic domains interact efficiently with the cytoplasmic subunits of the phagocyte NADPH oxidase and identify the second cytoplasmic loop of NOX electron transporters as a crucial domain for enzyme function. Studies of cytosolic co-factors showed that the C-terminal cytoplasmic domain of NOX1 was absolutely required for activation with NOXO1 and NOXA1 and that this activity required interaction of the putative NADPH-binding region of this domain with NOXA1. Finally, we have provided the first example of how alternative splicing of a NOX co-factor may be involved in the regulation of NADPH oxidase function.

Original languageEnglish (US)
Pages (from-to)S22-S23
JournalJapanese Journal of Infectious Diseases
Volume57
Issue number5
StatePublished - Oct 1 2004

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ASJC Scopus subject areas

  • Microbiology (medical)
  • Infectious Diseases

Cite this

Clark, R. A., Epperson, T. K., & Valente, A. J. (2004). Mechanisms of activation of NADPH oxidases. Japanese Journal of Infectious Diseases, 57(5), S22-S23.