Structural mechanism of intracellular autoregulation of zinc uptake in ZIP transporters

Changxu Pang, Jin Chai, Ping Zhu, John Shanklin and Qun Liu ()
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Changxu Pang: Brookhaven National Laboratory
Jin Chai: Brookhaven National Laboratory
Ping Zhu: Brookhaven National Laboratory
John Shanklin: Brookhaven National Laboratory
Qun Liu: Brookhaven National Laboratory

Nature Communications, 2023, vol. 14, issue 1, 1-10

Abstract: Abstract Zinc is an essential micronutrient that supports all living organisms through regulating numerous biological processes. However, the mechanism of uptake regulation by intracellular Zn2+ status remains unclear. Here we report a cryo-electron microscopy structure of a ZIP-family transporter from Bordetella bronchiseptica at 3.05 Å resolution in an inward-facing, inhibited conformation. The transporter forms a homodimer, each protomer containing nine transmembrane helices and three metal ions. Two metal ions form a binuclear pore structure, and the third ion is located at an egress site facing the cytoplasm. The egress site is covered by a loop, and two histidine residues on the loop interact with the egress-site ion and regulate its release. Cell-based Zn2+ uptake and cell growth viability assays reveal a negative regulation of Zn2+ uptake through sensing intracellular Zn2+ status using a built-in sensor. These structural and biochemical analyses provide mechanistic insight into the autoregulation of zinc uptake across membranes.

Date: 2023
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DOI: 10.1038/s41467-023-39010-6

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