SLC39A7 and cancer: This ZIP7-mediated zinc release requires phosphorylation by protein kinase CK2 on two serine residues (S275 and S276) on the long intracellular loop of ZIP7 between TM III and TM IV.16 We have now developed a unique monoclonal antibody which binds ZIP7 only when phosphorylated on these two serine residues17 and have demonstrated that the mobilisation of zinc induced by the activation of ZIP7 is involved in regulating growth factor signalling of many pathways known to be responsible for aggressive cancer growth.