Evolution of copper transporting ATPases in eukaryotic organisms
Arnab Gupta1, Svetlana Lutsenko
1Department of Physiology, Johns Hopkins University, Baltimore, MD 21205, USA.
Current Genomics
|October 2, 2012
Summary
Copper-ATPases maintain cellular copper balance. In eukaryotes, these proteins evolved distinct roles, supplying copper to enzymes and aiding detoxification, with N-terminal domains potentially driving this diversification.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Copper is essential but toxic in excess.
- Copper-ATPases are conserved membrane proteins regulating cellular copper.
- These proteins are vital across all life forms, from bacteria to humans.
Purpose of the Study:
- To review the origin and diversification of Copper-ATPases in eukaryotes.
- To explore the functional evolution of these essential proteins.
Main Methods:
- Review of existing literature on Copper-ATPase evolution.
- Comparative analysis of Copper-ATPase functions across eukaryotic taxa.
Main Results:
- Copper-ATPases have dual roles in eukaryotes: detoxification and supplying copper to secretory pathway enzymes.
- A divergence into two distinct Copper-ATPases occurred with the evolution of chordates.
- The N-terminal metal-binding domain is implicated in functional diversification.
Conclusions:
- Copper-ATPase evolution in eukaryotes led to specialized functions beyond simple detoxification.
- The diversification of Copper-ATPases is crucial for cellular copper homeostasis and function in complex organisms.
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