|ZFIN ID: ZDB-PUB-160610-8|
Zinc transporter ZIP10 forms a heteromer with ZIP6 which regulates embryonic development and cell migration
Taylor, K.M., Muraina, I., Brethour, D., Schmitt-Ulms, G., Nimmanon, T., Ziliotto, S., Kille, P., Hogstrand, C.
|Source:||The Biochemical journal 473(16): 2531-44 (Journal)|
|Keywords:||EMT, gastrulation, zebrafish, zinc signalling, zinc transporter (SLC39A10), zinc transporter (SLC39A6)|
|PubMed:||27274087 Full text @ Biochem. J.|
Taylor, K.M., Muraina, I., Brethour, D., Schmitt-Ulms, G., Nimmanon, T., Ziliotto, S., Kille, P., Hogstrand, C. (2016) Zinc transporter ZIP10 forms a heteromer with ZIP6 which regulates embryonic development and cell migration. The Biochemical journal. 473(16):2531-44.
ABSTRACTThere is growing evidence that zinc and its transporters are involved in cell migration during development and in cancer. In the present study, we show that zinc transporter ZIP10 (SLC39A10) stimulates cell motility and proliferation, both in mammalian cells and in the zebrafish embryo. This is associated with inactivation of GSK-3α and -3ß and downregulation of E-cadherin (CDH1). Morpholino-mediated knock-down of zip10 causes delayed epiboly and deformities of the head, eye, heart and tail. Furthermore, zip10 deficiency results in overexpression of cdh1, zip6 and stat3, the latter gene product driving transcription of both zip6 and zip10 The non-reduntant requirement of Zip6 and Zip10 for epithelial to mesenchymal transition (EMT) is consistent with our finding that they exist as a heteromer. We postulate that a subset of ZIPs carrying PrP-like ectodomains, including ZIP6 and ZIP10, are integral to cellular pathways and plasticity programs, such as EMT.