Abstract
A number of secretory, membrane-bound or organelle-resident enzymes are properly folded and become functional active forms by binding with zinc during their itinerary in the secretory pathway. Zinc homeostasis within the pathway, therefore, has to be strictly regulated. In vertebrate cells, it is regulated through the coordinated zinc mobilization by specific ZnT (Zn transporter, SLC30A) and ZIP (Zrt, Irt-related protein, SLC39A) transporters. This article reviews the recent progress in cellular and functional properties of such zinc transporters including those expressed in cell-specific manner, and shortly discusses future perspectives based on current data.
