N-linked glycosylation of the superoxide-producing NADPH oxidase Nox1

Kei Miyano, Hideki Sumimoto

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Nox1 is a membrane-integrated protein that belongs to the Nox family of superoxide-producing NADPH oxidases. Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively. Simultaneous threonine substitution for these residues completely abrogates the glycosylation, but does not prevent Nox1 from forming a heterodimer with p22phox, trafficking to the cell surface, or producing superoxide. In the absence of p22phox, Nox1 is transported to the plasma membrane mainly as a form with high mannose N-glycans, although their conversion into complex N-glycans is induced by expression of p22 phox. These findings indicate that glycosylation and subsequent N-glycan maturation of Nox1 are both dispensable for its cell surface recruitment. Superoxide production by unglycosylated Nox1 is largely dependent on p22phox, which is abrogated by glutamine substitution for Pro-156 in p22phox, a mutation leading to a defective interaction with the Nox1-activating protein Noxo1. Thus p22phox directly contributes to Nox1 activation in a glycosylation-independent manner, besides its significant role in Nox1 glycan maturation.

Original languageEnglish
Pages (from-to)1060-1065
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume443
Issue number3
DOIs
Publication statusPublished - Jan 17 2014

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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