Evolution of copper transporting ATPases in eukaryotic organisms

Arnab Gupta, Svetlana Lutsenko

Research output: Contribution to journalArticle

Abstract

Copper is an essential nutrient for most life forms, however in excess it can be harmful. The ATP-driven copper pumps (Copper-ATPases) play critical role in living organisms by maintaining appropriate copper levels in cells and tissues. These evolutionary conserved polytopic membrane proteins are present in all phyla from simplest life forms (bacteria) to highly evolved eukaryotes (Homo sapiens). The presumed early function in metal detoxification remains the main function of Copper-ATPases in prokaryotic kingdom. In eukaryotes, in addition to removing excess copper from the cell, Copper-ATPases have another equally important function - to supply copper to copper dependent enzymes within the secretory pathway. This review focuses on the origin and diversification of Copper ATPases in eukaryotic organisms. From a single Copper ATPase in protozoans, a divergence into two functionally distinct ATPases is observed with the evolutionary appearance of chordates. Among the key functional domains of Copper-ATPases, the metal-binding N-terminal domain could be responsible for functional diversification of the copper ATPases during the course of evolution.

Original languageEnglish (US)
Pages (from-to)124-133
Number of pages10
JournalCurrent Genomics
Volume13
Issue number2
DOIs
StatePublished - Apr 2012

Fingerprint

Copper
Adenosine Triphosphatases
Eukaryota
copper-transporting ATPases
Metals
Chordata
Secretory Pathway
Membrane Proteins
Adenosine Triphosphate
Bacteria
Food

Keywords

  • ATP7B
  • ATPase
  • CopA
  • Copper

ASJC Scopus subject areas

  • Genetics
  • Genetics(clinical)

Cite this

Evolution of copper transporting ATPases in eukaryotic organisms. / Gupta, Arnab; Lutsenko, Svetlana.

In: Current Genomics, Vol. 13, No. 2, 04.2012, p. 124-133.

Research output: Contribution to journalArticle

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