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Title of Journal: J Biol Inorg Chem

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Abbravation: JBIC Journal of Biological Inorganic Chemistry

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Springer-Verlag

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DOI

10.1016/0019-0578(90)90034-i

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1432-1327

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Human copper transporter Ctr1 is functional in Em

Authors: Haiqing Hua Oleg Georgiev Walter Schaffner Dominik Steiger
Publish Date: 2009/10/25
Volume: 15, Issue: 1, Pages: 107-
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Abstract

Living cells have to carefully control the intracellular concentration of trace metals especially of copper which is at the same time essential but owing to its redox activity can also facilitate generation of reactive oxygen species Mammals have two related copper transporters Ctr1 and Ctr2 with Ctr1 playing the major role The fruit fly Drosophila has three family members termed Ctr1A Ctr1B and Ctr1C Ctr1A is expressed throughout development and a null mutation causes lethality at an early stage Ctr1B ensures efficient copper uptake in the intestinal tract whereas Ctr1C is mainly expressed in male gonads Ectopic expression of Ctr1 transporters in Drosophila causes toxic effects due to excessive copper uptake Here we compare the effects of human Ctr1 hCtr1 with those of the Drosophila homologs Ctr1A and Ctr1B in two overexpression assays Whereas the overexpression of Drosophila Ctr1A and Ctr1B results in strong phenotypes expression of hCtr1 causes only a very mild phenotype indicating a low copperimport efficiency in the Drosophila system However this can be boosted by coexpressing the human copper chaperone CCS Surprisingly hCtr1 complements a lethal Ctr1A mutation at least as well as Ctr1A and Ctr1B transgenes These findings reveal a high level of conservation between the mammalian and insect Ctr1type copper importers and they also demonstrate that the Drosophila Ctr1 proteins are functionally interchangeableWe thank Michelle L Turski Dennis J Thiele Duke University Medical Center Johannes Bischof and Konrad Basler Zurich University for fly stocks and plasmids Till Strassen for help with stock keeping and George Hausmann for valuable comments on the manuscript

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