ATP-dependent copper transport by the Menkes protein in membrane vesicles isolated from cultured Chinese hamster ovary cells

FEBS Lett. 1998 Sep 18;435(2-3):178-82. doi: 10.1016/s0014-5793(98)01059-x.


The Menkes (MNK) protein is a vital component of copper homeostasis in mammalian cells. In this paper we provide the first biochemical evidence that the MNK protein functions as a copper-translocating P-type ATPase in mammalian cells. The enzyme activity in membrane vesicles prepared from Chinese hamster ovary cells overexpressing MNK was ATP-dependent, correlated with the amount of MNK and followed Michaelis-Menten kinetics with respect to copper. The copper transport was observed only under reducing conditions suggesting MNK transports Cu(I). This study opens the way to detailed structure-function studies and assessment of functional MNK derived from patients with Menkes disease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Adenosine Triphosphate / metabolism
  • Animals
  • CHO Cells
  • Carrier Proteins / metabolism*
  • Cation Transport Proteins*
  • Cell Membrane / metabolism*
  • Cell Membrane / ultrastructure
  • Copper / metabolism*
  • Cricetinae
  • Cytoplasmic Granules / metabolism*
  • Ion Transport
  • Recombinant Fusion Proteins*


  • Carrier Proteins
  • Cation Transport Proteins
  • Recombinant Fusion Proteins
  • Copper
  • Adenosine Triphosphate
  • Adenosine Triphosphatases