We are analyzing https://link.springer.com/article/10.1007/s10534-011-9438-1.

Title:
Distorted copper homeostasis with decreased sensitivity to cisplatin upon chaperone Atox1 deletion in Drosophila | BioMetals
Description:
Copper is an integral part of a number of proteins and thus an essential trace metal. However, free copper ions can be highly toxic and every organism has to carefully control its bioavailability. Eukaryotes contain three copper chaperones; Atx1p/Atox1 which delivers copper to ATP7 transporters located in the trans-Golgi network, Cox17 which provides copper to the mitochondrial cytochrome c oxidase, and CCS which is a copper chaperone for superoxide dismutase 1. Here we describe the knockout phenotype of the Drosophila homolog of mammalian Atox1 (ATX1 in yeast). Atox1−/− flies develop normally, though at reduced numbers, and the eclosing flies are fertile. However, the mutants are unable to develop on low-copper food. Furthermore, the intestinal copper importer Ctr1B, which is regulated by copper demand, fails to be induced upon copper starvation in Atox1−/− larvae. At the same time, intestinal metallothionein is upregulated. This phenotype, which resembles the one of the ATP7 mutant, is best explained by intestinal copper accumulation, combined with insufficient delivery to the rest of the body. In addition, compared to controls, Drosophila Atox1 mutants are relatively insensitive to the anticancer drug cisplatin, a compound which is also imported via Ctr1 copper transporters and was recently found to bind mammalian Atox1.
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Keywords {🔍}

copper, article, pubmed, google, scholar, cas, biol, drosophila, chem, atox, transporter, cisplatin, chaperone, thiele, schaffner, essential, homeostasis, georgiev, human, proc, natl, acad, sci, superoxide, molecular, mechanisms, privacy, cookies, content, hua, dismutase, ctr, access, role, zürich, information, publish, search, günther, metal, cox, yeast, intestinal, cells, balamurugan, camakaris, biochem, mercer, med, culotta,

Topics {✒️}

germ-line-specific phic31 integrases month download article/chapter beta-globin mrna precursor copper-mediated intracellular trafficking metal-responsive transcription factor oleg georgiev & walter schaffner copper-regulated transporter required article biometals aims ctr1-mediated copper distorted copper homeostasis full article pdf related subjects free copper ions privacy choices/manage cookies human copper chaperone copper transporter ctr1 drosophila ctr1a functions influx transporter hctr1 human copper transporters ctr1 copper transporters anticancer drug cisplatin metal ions essential trace metal copper transporter family copper transporter essential specific copper transfer perinatal copper homeostasis bind mammalian atox1 drosophila metallothioneins reveals optimized transgenesis system intracellular shuttle service chaperone atox1 deletion copper-transport diseases low-copper food intracellular copper transport copper chaperone atx1 copper chaperone cox17 intestinal copper accumulation european economic area trans-golgi network app23 transgenic mice mercer jf speck-martins ce turski ml berk-sharp procedure identical map coordinates article hua metallochaperone atox1 plays conditions privacy policy flies carrying transposase

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         description:Copper is an integral part of a number of proteins and thus an essential trace metal. However, free copper ions can be highly toxic and every organism has to carefully control its bioavailability. Eukaryotes contain three copper chaperones; Atx1p/Atox1 which delivers copper to ATP7 transporters located in the trans-Golgi network, Cox17 which provides copper to the mitochondrial cytochrome c oxidase, and CCS which is a copper chaperone for superoxide dismutase 1. Here we describe the knockout phenotype of the Drosophila homolog of mammalian Atox1 (ATX1 in yeast). Atox1−/− flies develop normally, though at reduced numbers, and the eclosing flies are fertile. However, the mutants are unable to develop on low-copper food. Furthermore, the intestinal copper importer Ctr1B, which is regulated by copper demand, fails to be induced upon copper starvation in Atox1−/− larvae. At the same time, intestinal metallothionein is upregulated. This phenotype, which resembles the one of the ATP7 mutant, is best explained by intestinal copper accumulation, combined with insufficient delivery to the rest of the body. In addition, compared to controls, Drosophila Atox1 mutants are relatively insensitive to the anticancer drug cisplatin, a compound which is also imported via Ctr1 copper transporters and was recently found to bind mammalian Atox1.
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      description:Copper is an integral part of a number of proteins and thus an essential trace metal. However, free copper ions can be highly toxic and every organism has to carefully control its bioavailability. Eukaryotes contain three copper chaperones; Atx1p/Atox1 which delivers copper to ATP7 transporters located in the trans-Golgi network, Cox17 which provides copper to the mitochondrial cytochrome c oxidase, and CCS which is a copper chaperone for superoxide dismutase 1. Here we describe the knockout phenotype of the Drosophila homolog of mammalian Atox1 (ATX1 in yeast). Atox1−/− flies develop normally, though at reduced numbers, and the eclosing flies are fertile. However, the mutants are unable to develop on low-copper food. Furthermore, the intestinal copper importer Ctr1B, which is regulated by copper demand, fails to be induced upon copper starvation in Atox1−/− larvae. At the same time, intestinal metallothionein is upregulated. This phenotype, which resembles the one of the ATP7 mutant, is best explained by intestinal copper accumulation, combined with insufficient delivery to the rest of the body. In addition, compared to controls, Drosophila Atox1 mutants are relatively insensitive to the anticancer drug cisplatin, a compound which is also imported via Ctr1 copper transporters and was recently found to bind mammalian Atox1.
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         Microbiology
         Cell Biology
         Plant Physiology
         Medicine/Public Health
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