Abstract
ZIP transporters, named after the zinc regulated (Zrt) and iron regulated (Irt) transport proteins, are essential for zinc and iron translocation across cellular membranes. These proteins function to increase the cytosolic concentration of transition metals. While both zinc and iron are essential micronutrients which are required for the structure and/or function of hundreds of cellular proteins, the molecular mechanism of ZIP transporters is not well understood. Complicating mechanistic studies is the observation that the concentration of free zinc and iron is nano to picomolar. Our interest has been to elucidate the mechanism of zinc transport mediated by the human (h) ZIP4. hZIP4 is located at the primary location of zinc uptake in humans and has been directly implicated in multiple disease states including Acrodermatitis enteropathica and pancreatic cancer. However the mechanism of transport is not known. We have previously shown that zinc, nickel and copper can be transported by hZIP4, following heterologous expression in X. laevis oocytes, where there are two binding affinities (in the nM and μM range of biometal). Currently, our research interests have been to target residues of functional importance. Here, we will describe some of our recent efforts.
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