Integrating trace element metabolism from the cell to the whole organism.
The redox chemistry of copper (Cu) makes this both a powerful enzyme catalyst and a dangerous reactant that generates hydroxyl radical. Although virtually all cells from microbes to mammals must acquire Cu to drive important biochemical reactions, the potential toxicity of Cu demands an exquisite level of vectorial transport and homeostatic control. Our laboratory is interested in how organisms acquire Cu through the action of high-affinity plasma membrane Cu transporters of the copper transport protein (Ctr) class of proteins. We have isolated Ctr Cu transporters from baker's yeast and fission yeast and from flies, mice and mammals. This review will focus on understanding how the Ctr high-affinity Cu transport proteins function, from their biochemical mechanism of action in yeast and cultured metazoan cells to their roles in Cu delivery and mammalian embryonic development.
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0606, USA. dthiele@umich.edu
Dennis J
DJ
Thiele
D000818:Animals; D001692:Biological Transport; D002477:Cells / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D006706:Homeostasis; D006801:Humans; D008954:Models, Biological; D014131:Trace Elements / Q000378:metabolism*
D014131:Trace Elements; D003300:Copper