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18 reviewsSUMMARYZinc is an essential micronutrient that regulates a wide range of physiological processes, most often throughzinc binding to protein cysteine residues. Despite being critical for modulation of protein function, thecysteine sites in the majority of the human proteome that are subject to zinc binding remain undefined.Here, we develop ZnCPT, a deep and quantitative mapping of the zinc-binding cysteine proteome. We define6,173 zinc-binding cysteines, uncovering protein families across major domains of biology that are subject toconstitutive or inducible zinc binding. ZnCPT enables systematic discovery of zinc-regulated structural,enzymatic, and allosteric functional domains. On this basis, we identify 52 cancer genetic dependencies subject to zinc binding and nominate malignancies sensitive to zinc-induced cytotoxicity. We discover a mechanism of zinc regulation over glutathione reductase (GSR), which drives cell death in GSR-dependent lungcancers. We provide ZnCPT as a resource for understanding mechanisms of zinc regulation of proteinfunction.
