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Arch Biochem Biophys. 2007 Jul 15;463(2):134-48. Epub 2007 May 2.

Biochemical basis of regulation of human copper-transporting ATPases.

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1
Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, OR 97239, USA. lutsenko@ohsu.edu

Abstract

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 ATP7B. 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 intracellular 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.

PMID:
17562324
PMCID:
PMC2025638
DOI:
10.1016/j.abb.2007.04.013
[Indexed for MEDLINE]
Free PMC Article
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