Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-36740
Hua, H; Georgiev, O; Schaffner, W; Steiger, D (2010). Human copper transporter Ctr1 is functional in Drosophila, revealing a high degree of conservation between mammals and insects. Journal of Biological Inorganic Chemistry, 15(1):107-113.
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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 copper-import 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 Ctr1-type copper importers, and they also demonstrate that the Drosophila Ctr1 proteins are functionally interchangeable.
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|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||07 Faculty of Science > Institute of Molecular Life Sciences|
|DDC:||570 Life sciences; biology|
|Deposited On:||05 Nov 2010 09:45|
|Last Modified:||15 Jan 2014 14:42|
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