Molecular mechanisms of copper uptake and distribution.
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.
Puig
Sergi
S
Department of Biological Chemistry, University of Michigan Medical School, 1301 Catherine Road, Ann Arbor, Michigan 48109-0606, USA.
Thiele
Dennis J
DJ
D000818:Animals; D017920:Antiporters / Q000378:metabolism; D001692:Biological Transport; D027682:Cation Transport Proteins; D003300:Copper / Q000493:pharmacokinetics*; D000079923:Copper Transporter 1; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008667:Metalloproteins / Q000378:metabolism; D000080083:SLC31 Proteins; D029701:Saccharomyces cerevisiae Proteins; D015003:Yeasts
D017920:Antiporters; C100982:CTR3 protein, S cerevisiae; D027682:Cation Transport Proteins; D000079923:Copper Transporter 1; D008565:Membrane Proteins; D008667:Metalloproteins; D000080083:SLC31 Proteins; C490079:SLC31A1 protein, human; D029701:Saccharomyces cerevisiae Proteins; C490077:Slc31a1 protein, mouse; D003300:Copper