Research ArticleHOST DEFENSE

Ubiquitination of STING at lysine 224 controls IRF3 activation

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Science Immunology  05 May 2017:
Vol. 2, Issue 11, eaah7119
DOI: 10.1126/sciimmunol.aah7119

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Fine-tuning the STING

In eukaryotic cells, cytosolic DNA is often an indicator of viral infection. STING (stimulator of interferon genes), an endoplasmic reticulum–associated protein, is a central node that connects cytosolic DNA sensing with transcription factors (such as interferon regulatory factors) that drive antiviral host responses. STING activation is tightly regulated. Chronic STING activation has been documented in autoinflammatory settings, whereas STING agonists are being considered as a means to activate innate immune responses to cancers. Here, Ni et al. show that MUL1 (mitochondrial E3 ubiquitin protein ligase 1) ubiquitinates STING at lysine 224 to promote STING-dependent production of antiviral cytokines and chemokines. By extending our understanding of STING activation, these studies may lead to new approaches to modulating STING activation in various settings.