Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 463, Issue 2, Pages 134-148Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2007.04.013
Keywords
ATP7A; ATP7B; copper; P-type ATPase; atox1
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Funding
- NHLBI NIH HHS [T32 HL007781, 5-T32-HL007781] Funding Source: Medline
- NIDDK NIH HHS [R01 DK071865-02, R01 DK071865] Funding Source: Medline
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Copper is essential for cell metabolism as a cofactor of key metabolic enzymes. The biosynthetic incorporation of copper into secreted and plasma membrane-bound proteins requires activity of the copper-transporting ATPases (Cu-ATPases) ATP7A and ATP713. The Cu-ATPases also export excess copper from the cell and thus critically contribute to the homeostatic control of copper. The trafficking of Cu-ATPases from the trans-Golgi network to endocytic vesicles in response to various signals allows for the balance between the biosynthetic and copper exporting functions of these transporters. Although significant progress has been made towards understanding the biochemical characteristics of human Cu-ATPase, the mechanisms that control their function and mtracellular localization remain poorly understood. In this review, we summarize current information on structural features and functional properties of ATP7A and ATP7B. We also describe sequence motifs unique for each Cu-ATPase and speculate about their role in regulating ATP7A and ATP7B activity and trafficking. (C) 2007 Elsevier Inc. All rights reserved.
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