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The Caenorhabditis elegans homolog of human copper chaperone Atox1, CUC-1, aids in distal tip cell migration
- Source :
- Biometals
- Publication Year :
- 2020
- Publisher :
- Springer Science and Business Media LLC, 2020.
-
Abstract
- Cell migration is a fundamental biological process involved in for example embryonic development, immune system and wound healing. 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. 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. elegans gonad. 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. 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. Importantly, the distal tip cell migration defect was rescued by a wild-type cuc-1 transgene provided to cuc-1 knock-out worms. The results obtained here for C. elegans CUC-1 imply that Atox1 homologs, in addition to their well-known cytoplasmic copper transport, may contribute to developmental cell migration processes.
- Subjects :
- 0301 basic medicine
Transgene
CUC-1
Article
General Biochemistry, Genetics and Molecular Biology
Biomaterials
ATOX1
03 medical and health sciences
0302 clinical medicine
Copper Transport Proteins
Cell Movement
Distal tip cell migration
Animals
Humans
Cell migration
Caenorhabditis elegans
Caenorhabditis elegans Proteins
biology
Embryogenesis
Metals and Alloys
Copper transport
biology.organism_classification
Cell biology
030104 developmental biology
Atox1
Cytoplasm
030220 oncology & carcinogenesis
Chaperone (protein)
biology.protein
General Agricultural and Biological Sciences
Copper
Molecular Chaperones
Subjects
Details
- ISSN :
- 15728773 and 09660844
- Volume :
- 33
- Database :
- OpenAIRE
- Journal :
- BioMetals
- Accession number :
- edsair.doi.dedup.....39ef8190843d17006442b15c8f705dee