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Here, we show that the <jats:italic>bona fide<\/jats:italic> nonglycoprotein Nox5, a transmembrane superoxide\u2010producing NADPH oxidase, is transported to the cell surface in a manner resistant to co\u2010expression of Sar1 (H79G), a GTP\u2010fixed mutant of the small GTPase Sar1, which blocks COPII vesicle fission from the ER. In contrast, Sar1 (H79G) effectively inhibits ER\u2010to\u2010Golgi transport of glycoproteins including the Nox5\u2010related oxidase Nox2. The trafficking of Nox2, but not that of Nox5, is highly sensitive to over\u2010expression of syntaxin 5 (Stx5), a t\u2010SNARE required for COPII ER\u2010to\u2010Golgi transport. Thus, Nox2 and Nox5 mainly traffic via the Sar1\/Stx5\u2010dependent and\u00a0\u2010independent pathways, respectively. Both participate in Nox1 trafficking, as Nox1 advances to the cell surface in two differentially <jats:italic>N<\/jats:italic>\u2010glycosylated forms, one complex and one high mannose, in a Sar1\/Stx5\u2010dependent and\u00a0\u2010independent manner, respectively. Nox2 and Nox5 also can use both pathways: a glycosylation\u2010defective mutant Nox2 is weakly recruited to the plasma membrane in a less Sar1\u2010dependent manner; <jats:italic>N<\/jats:italic>\u2010glycosylated Nox5 mutants reach the cell surface in part as the complex form Sar1\u2010dependently, albeit mainly as the high\u2010mannose form in a Sar1\u2010independent manner.<\/jats:p>","DOI":"10.1111\/gtc.12590","type":"journal-article","created":{"date-parts":[[2018,5,2]],"date-time":"2018-05-02T14:19:39Z","timestamp":1525270779000},"page":"480-493","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Differential cell surface recruitment of the superoxide\u2010producing NADPH oxidases Nox1, Nox2 and Nox5: The role of the small GTPase 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