Atox1 contains positive residues that mediate membrane association and aid subsequent copper loading

Adrian G. Flores, Vinzenz M. Unger*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Copper chaperones bind intracellular copper and ensure proper trafficking to downstream targets via protein-protein interactions. In contrast to the mechanisms of copper binding and transfer to downstream targets, the mechanisms of initial copper loading of the chaperones are largely unknown. Here, we demonstrate that antioxidant protein 1 (Atox1 in human cells), the principal cellular copper chaperone responsible for delivery of copper to the secretory pathway, possesses the ability to interact with negatively charged lipid headgroups via distinct surface lysine residues. Moreover, loss of these residues lowers the efficiency of copper loading of Atox1 in vivo, suggesting that the membrane may play a scaffolding role in copper distribution to Atox1. These findings complement the recent discovery that the membrane also facilitates copper loading of the copper chaperone for superoxide dismutase 1 and provide further support for the emerging paradigm that the membrane bilayer plays a central role in cellular copper acquisition and distribution.

Original languageEnglish (US)
Pages (from-to)903-913
Number of pages11
JournalJournal of Membrane Biology
Issue number12
StatePublished - Dec 2013


  • Atox1
  • Chaperone
  • Copper homeostasis
  • Copper trafficking
  • Membrane scaffold

ASJC Scopus subject areas

  • Biophysics
  • Physiology
  • Cell Biology


Dive into the research topics of 'Atox1 contains positive residues that mediate membrane association and aid subsequent copper loading'. Together they form a unique fingerprint.

Cite this