Structural organization of human Cu-transporting ATPases

Learning from building blocks

Amanda N. Barry, Ujwal Shinde, Svetlana Lutsenko

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

Copper-transporting ATPases (Cu-ATPases) ATP7A and ATP7B play an essential role in human physiological function. Their primary function is to deliver copper to the secretory pathway and export excess copper from the cell for removal or further utilization. Cells employ Cu-ATPases in numerous physiological processes that include the biosynthesis of copper-dependent enzymes, lactation, and response to hypoxia. Biochemical studies of human Cu-ATPases and their orthologs have demonstrated that Cu-ATPases share many common structural and mechanistic characteristics with other members of the P-type ATPase family. Nevertheless, the Cu-ATPases have a unique coordinate environment for their ligands, copper and ATP, and additional domains that are required for sophisticated regulation of their intracellular localization and activity. Here, we review recent progress that has been made in understanding the structure of Cu-ATPases from the analysis of their individual domains and orthologs from microorganisms, and speculate about the implications of these findings for the function and regulation of human copper pumps.

Original languageEnglish (US)
Pages (from-to)47-59
Number of pages13
JournalJournal of Biological Inorganic Chemistry
Volume15
Issue number1
DOIs
StatePublished - Jan 2010
Externally publishedYes

Fingerprint

Adenosine Triphosphatases
Learning
Copper
Physiological Phenomena
Secretory Pathway
Biosynthesis
Lactation
Microorganisms
Adenosine Triphosphate
Pumps
Ligands
Enzymes

Keywords

  • ATP7A
  • ATP7B
  • CopA
  • Copper
  • P-type ATPase

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Structural organization of human Cu-transporting ATPases : Learning from building blocks. / Barry, Amanda N.; Shinde, Ujwal; Lutsenko, Svetlana.

In: Journal of Biological Inorganic Chemistry, Vol. 15, No. 1, 01.2010, p. 47-59.

Research output: Contribution to journalArticle

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