PUBLICATION

Zinc transporter ZIP10 forms a heteromer with ZIP6 which regulates embryonic development and cell migration

Authors
Taylor, K.M., Muraina, I., Brethour, D., Schmitt-Ulms, G., Nimmanon, T., Ziliotto, S., Kille, P., Hogstrand, C.
ID
ZDB-PUB-160610-8
Date
2016
Source
The Biochemical journal   473(16): 2531-44 (Journal)
Registered Authors
Keywords
EMT, gastrulation, zebrafish, zinc signalling, zinc transporter (SLC39A10), zinc transporter (SLC39A6)
MeSH Terms
  • Animals
  • CHO Cells
  • Cation Transport Proteins/classification
  • Cation Transport Proteins/metabolism*
  • Cell Adhesion
  • Cell Movement*
  • Cell Proliferation
  • Clustered Regularly Interspaced Short Palindromic Repeats
  • Cricetulus
  • Embryonic Development*
  • Epithelial-Mesenchymal Transition
  • Female
  • Humans
  • MCF-7 Cells
  • Male
  • Phylogeny
  • Zebrafish/embryology
  • Zinc/metabolism*
PubMed
27274087 Full text @ Biochem. J.
Abstract
There 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.
Genes / Markers
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Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
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Mapping