Research ArticleImmunology

Pinpointing cysteine oxidation sites by high-resolution proteomics reveals a mechanism of redox-dependent inhibition of human STING

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Science Signaling  27 Apr 2021:
Vol. 14, Issue 680, eaaw4673
DOI: 10.1126/scisignal.aaw4673

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Taking out the STING

The adaptor protein STING is stimulated in response to the detection of cytosolic viral DNA by the enzyme cGAS. STING activation then leads to the expression of genes encoding type I interferons as part of the antiviral response. STING activation also plays a role in antitumor immunity, making it an important therapeutic target. Zamorano Cuervo et al. used mass spectrometry and structural analyses to identify cysteine residues in STING that underwent reversible oxidation. One specific residue was oxidized in response to oxidants or a natural STING agonist, which the authors propose limits STING activity. Together, these findings may help in the design of therapeutics to modulate STING activity in the context of immunotherapies and vaccines.

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