Abstract
Copper is an essential yet toxic metal ion. To satisfy cellular requirements, while, at the same time, minimizing toxicity, complex systems of copper trafficking have evolved in all cell types. The best conserved and most widely distributed of these involve Atx1-like chaperones and P(1B)-type ATPase transporters. Here, we discuss current understanding of how these chaperones bind Cu(I) and transfer it to the Atx1-like N-terminal domains of their cognate transporter.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cation Transport Proteins / metabolism*
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Copper / chemistry
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Copper / metabolism*
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Copper Transport Proteins
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Homeostasis
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Humans
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Metallochaperones
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Models, Molecular
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Molecular Chaperones / chemistry
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism*
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Protein Conformation
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Trans-Activators / chemistry
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Trans-Activators / genetics
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Trans-Activators / metabolism
Substances
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ATOX1 protein, human
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ATX1 protein, S cerevisiae
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Bacterial Proteins
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Carrier Proteins
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Cation Transport Proteins
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CopZ protein, Enterococcus hirae
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Copper Transport Proteins
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Metallochaperones
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Molecular Chaperones
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Saccharomyces cerevisiae Proteins
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Trans-Activators
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Copper
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Adenosine Triphosphatases