Ca2+ -binding-region-dependent cell surface localization of NADPH oxidase Nox5.
FEBS Lett
; 597(5): 702-713, 2023 03.
Article
em En
| MEDLINE
| ID: mdl-36653838
ABSTRACT
Six gene splice variants of superoxide-generating NADPH oxidase 5 (Nox5) have been identified in humans, and they differ in the sequence of their N-terminal cytoplasmic domains, which comprise four EF-hand motifs. Here, we demonstrated that the Ca2+ -dependent association and dissociation between the N- and C-terminal cytoplasmic domains of the Nox5ß variant are affected by the alanine substitution of the conserved Ile-113 or Leu-115 at the connecting loop between the third and fourth EF-hand motifs. These substitutions impair the cell surface localization of Nox5ß. In addition, the Nox5ε/S variant, lacking all EF-hand motifs, does not localize to the plasma membrane. Thus, the Ca2+ -sensitive intramolecular interaction determines the Nox5 subcellular localization, that is, whether Nox5 variants generate superoxide in the extracellular or intracellular space.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
NADPH Oxidases
/
Proteínas de Membrana
Limite:
Humans
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2023
Tipo de documento:
Article
País de afiliação:
Japão