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Review
. 2009 Jan 9;284(2):717-21.
doi: 10.1074/jbc.R800055200. Epub 2008 Aug 29.

New roles for copper metabolism in cell proliferation, signaling, and disease

Michelle L Turski  1 , Dennis J Thiele
Affiliations
Review

New roles for copper metabolism in cell proliferation, signaling, and disease

Michelle L Turski et al. J Biol Chem. .
No abstract available

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Figures

FIGURE 1.
FIGURE 1.
Mammalian intracellular copper homeostasis. Copper is reduced by an as yet unidentified reductase and imported into cells by the high affinity copper transporter Ctr1. Once inside the cell, copper is escorted to destinations via the action of copper chaperones. CCS incorporates copper into the cytosolic protein Cu,Zn-SOD. Atox1 delivers copper to the secretory compartment; the protein possesses an N-terminal copper-binding motif (CXXC) that directly interacts with the N-terminal copper-binding domain of ATP7A and ATP7B (MTCXXC), facilitating copper delivery to ATP7A and ATP7B. ATP7A and ATP7B are P-type copper-transporting proteins that transport copper into the lumen of the Golgi, where the metal can then be incorporated into copper-dependent proteins such as the secreted form of LOX. The P-type ATPases also export copper out of the cell by translocating to the plasma membrane when intracellular copper levels are high. Copper is escorted to the mitochondria by an as yet uncharacterized ligand. Once inside the intermembrane space, copper is handed off to Cox17 and then passed onto either Sco1, which transfers copper to the Cox2 subunit of cytochrome oxidase, or Cox11, which transfers copper to the Cox1 subunit of cytochrome oxidase (CCO). TGN, trans-Golgi network; ER, endoplasmic reticulum.
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References

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