An expanding range of functions for the copper chaperone/antioxidant protein Atox1.

ABSTRACT:

Significance

Antioxidant protein 1 (Atox1 in human cells) is a copper chaperone for the copper export pathway with an essential role in cellular copper distribution. In vitro, Atox1 binds and transfers copper to the copper-transporting ATPases, stimulating their catalytic activity. Inactivation of Atox1 in cells inhibits maturation of secreted cuproenzymes as well as copper export from cells.

Recent advances

Accumulating data suggest that cellular functions of Atox1 are not limited to its copper-trafficking role and may include storage of labile copper, modulation of transcription, and antioxidant defense. The conserved metal binding site of Atox1, CxGC, differs from the metal-binding sites of copper-transporting ATPases and has a physiologically relevant redox potential tha

SUBMITTER: Hatori Y 

PROVIDER: S-EPMC3763234 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature