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Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, MI 48109-0606
2To whom correspondence should be addressed
The cellular uptake and intracellular distribution of the essential but highly toxic nutrient, copper, is a precisely orchestrated process. Copper homeostasis is coordinated by several proteins to ensure that it is delivered to specific subcellular compartments and copper-requiring proteins without releasing free copper ions that will cause damage to cellular components. Genetic studies in prokaryotic organisms and yeast have identified membrane-associated proteins that mediate the uptake or export of copper from cells. Within cells, small cytosolic proteins, called copper chaperones, have been identified that bind copper ions and deliver them to specific compartments and copper-requiring proteins. The identification of mammalian homologues of these proteins reveal a remarkable structural and functional conservation of copper metabolism between bacteria, yeast and humans. Furthermore, studies on the function and localization of the products of the Menkes and Wilson's disease genes, which are defective in patients afflicted with these diseases, have provided valuable insight into the mechanisms of copper balance and their role in maintaining appropriate copper distribution in mammals.
KEY WORDS: • copper • transport • distribution • Menkes • Wilson's disease • homeostatic regulation
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J. Beaudoin and S. Labbe The Fission Yeast Copper-sensing Transcription Factor Cuf1 Regulates the Copper Transporter Gene Expression through an Ace1/Amt1-like Recognition Sequence J. Biol. Chem., April 27, 2001; 276(18): 15472 - 15480. [Abstract] [Full Text] [PDF]
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H. Zhou and D. J. Thiele Identification of a Novel High Affinity Copper Transport Complex in the Fission Yeast Schizosaccharomyces pombe J. Biol. Chem., June 1, 2001; 276(23): 20529 - 20535. [Abstract] [Full Text] [PDF]
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S. M. Vanderwerf, M. J. Cooper, I. V. Stetsenko, and S. Lutsenko Copper Specifically Regulates Intracellular Phosphorylation of the Wilson's Disease Protein, a Human Copper-transporting ATPase J. Biol. Chem., September 21, 2001; 276(39): 36289 - 36294. [Abstract] [Full Text] [PDF]
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I. Voskoboinik, J. Mar, D. Strausak, and J. Camakaris The Regulation of Catalytic Activity of the Menkes Copper-translocating P-type ATPase. ROLE OF HIGH AFFINITY COPPER-BINDING SITES J. Biol. Chem., July 20, 2001; 276(30): 28620 - 28627. [Abstract] [Full Text] [PDF]
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F. W. Outten, D. L. Huffman, J. A. Hale, and T. V. O'Halloran The Independent cue and cus Systems Confer Copper Tolerance during Aerobic and Anaerobic Growth in Escherichia coli J. Biol. Chem., August 10, 2001; 276(33): 30670 - 30677. [Abstract] [Full Text] [PDF]
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F. Arnesano, L. Banci, I. Bertini, F. Cantini, S. Ciofi-Baffoni, D. L. Huffman, and T. V. O'Halloran Characterization of the Binding Interface between the Copper Chaperone Atx1 and the First Cytosolic Domain of Ccc2 ATPase J. Biol. Chem., October 26, 2001; 276(44): 41365 - 41376. [Abstract] [Full Text] [PDF]
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L. A. Meyer, A. P. Durley, J. R. Prohaska, and Z. L. Harris Copper Transport and Metabolism Are Normal in Aceruloplasminemic Mice J. Biol. Chem., September 21, 2001; 276(39): 36857 - 36861. [Abstract] [Full Text] [PDF]
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E. C. Theil and R. S. Eisenstein Combinatorial mRNA Regulation: Iron Regulatory Proteins and Iso-iron-responsive Elements (Iso-IREs) J. Biol. Chem., December 22, 2000; 275(52): 40659 - 40662. [Full Text] [PDF]
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