Molecular mechanisms of copper uptake and distribution

Curr Opin Chem Biol. 2002 Apr;6(2):171-80. doi: 10.1016/s1367-5931(02)00298-3.


In the past few years, exciting advances have been made toward understanding how copper is transported into and distributed to cupro-proteins within cells. Recent work has identified high-affinity copper transporters at the plasma membrane in a number of organisms. The elucidation of the three-dimensional structure of copper chaperones and target cupro-proteins has shown that highly specific interactions between homologous domains foster copper transfer between conserved copper ligands, and facilitate a detailed understanding of vectorial copper-transfer reactions. Furthermore, the recent generation of mouse-knockout models, deficient in a high-affinity copper transporter, or in copper chaperones, has demonstrated the importance of copper uptake and targeted distribution in both predicted and fascinating unanticipated ways in growth and development.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Antiporters / metabolism
  • Biological Transport
  • Cation Transport Proteins*
  • Copper / pharmacokinetics*
  • Copper Transporter 1
  • Humans
  • Membrane Proteins / metabolism
  • Metalloproteins / metabolism
  • SLC31 Proteins
  • Saccharomyces cerevisiae Proteins*
  • Yeasts


  • Antiporters
  • CTR3 protein, S cerevisiae
  • Cation Transport Proteins
  • Copper Transporter 1
  • Membrane Proteins
  • Metalloproteins
  • SLC31 Proteins
  • SLC31A1 protein, human
  • Saccharomyces cerevisiae Proteins
  • Slc31a1 protein, mouse
  • Copper