Atx1-like chaperones and their cognate P-type ATPases: copper-binding and transfer

作者：Singleton Chloe; Le Brun Nick E^*

来源：Biometals, 2007, 20(3-4): 275-289.

DOI：10.1007/s10534-006-9068-1

• copper trafficking
• chaperone
• P-type ATPase
• copper transfer
• Atx1
• CopZ

Copper is an essential yet toxic metal ion. To satisfy cellular requirements, while, at the same time, minimizing toxicity, complex systems of copper trafficking have evolved in all cell types. The best conserved and most widely distributed of these involve Atx1-like chaperones and P-1B-type ATPase transporters. Here, we discuss current understanding of how these chaperones bind Cu(I) and transfer it to the Atx1-like N-terminal domains of their cognate transporter.

• 出版日期2007-6