![]() In human cells, after copper transporter protein 1 (Ctr1)-mediated uptake, the cytoplasmic Cu chaperone Atox1 transports Cu to ATP7A and ATP7B in the trans-Golgi network (Puig and Thiele 2002). In order to avoid toxicity of free Cu ions, intracellular Cu is regulated by devoted Cu transport proteins that assist uptake, efflux, and distribution of the metal ion to load Cu-dependent proteins (Festa and Thiele 2011 Matson Dzebo et al. elegans CUC-1 imply that Atox1 homologs, in addition to their well-known cytoplasmic copper transport, may contribute to developmental cell migration processes.Ĭopper (Cu) is an essential nutrient in living organisms acting as a cofactor in proteins facilitating for example respiration, iron transport, oxidative stress protection, peptide hormone production, pigmentation, and blood clotting (Puig and Thiele 2002 Matson Dzebo et al. Importantly, the distal tip cell migration defect was rescued by a wild-type cuc-1 transgene provided to cuc-1 knock-out worms. Upon scoring of gonads, we found that cuc-1 knock-out, but not wild-type, worms exhibited distal tip cell migration defects in approximately 10–15% of animals and, had a significantly reduced brood size. ![]() Using knock-out worms, in which the cuc-1 gene was removed by CRISPR-Cas9 technology, we probed life span, brood size, as well as distal tip cell migration in the absence or presence of supplemented copper. To explore the role of the copper chaperone in other cell migration processes, we here investigated the putative involvement of an Atox1 homolog in Caenorhabditis elegans, CUC-1, in distal tip cell migration, which is a key process during the development of the C. Cell migration is also a key step in cancer metastasis and the human copper chaperone Atox1 was recently found to facilitate this process in breast cancer cells. ![]() ![]() Cell migration is a fundamental biological process involved in for example embryonic development, immune system and wound healing.
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