The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Cyclic di-GMP Sensing via the Innate Immune Signaling Protein STING
Open accessAbstract
SUMMARY Detection of foreign materials is the first step of successful immune responses. Stimulator of interferon genes (STING) was shown to directly bind cyclic diguanylate monophosphate (c-di-GMP), a bacterial second messenger, and to elicit strong interferon responses. Here we elucidate the structural features of the cytosolic c-di-GMP binding domain (CBD) of STING and its complex with c-di-GMP. The CBD exhibits an α + β fold and is a dimer in the crystal and in solution. Surprisingly, one c-di-GMP molecule binds to the central crevice of a STING dimer, using a series of stacking and hydrogen bonding interactions. We show that STING is autoinhibited by an intramolecular interaction between the CBD and the C-terminal tail (CTT) and that c-di-GMP releases STING from this autoinhibition by displacing the CTT. The structures provide a remarkable example of pathogen-host interactions in which a unique microbial molecule directly engages the innate immune system.
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Cites
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STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
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InfluentialAIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
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STING is a direct innate immune sensor of cyclic di-GMP
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Cited by
Regulation and function of the cGAS–STING pathway of cytosolic DNA sensing
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Innate Immune Pattern Recognition: A Cell Biological Perspective
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DNA sensing by the cGAS–STING pathway in health and disease
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Metadata
- Authors
- Yin, Q., Tian, Y., Kabaleeswaran, V., Jiang, X., Tu, D., Eck, M. J., Chen, Z. J., & Wu, H.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2012-06
- Volume
- 46
- Issue
- 6
- Pages
- 735-745
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2116527093
- Cited by
- 278
- References
- 10
- FWCI
- 8.50
- Type
- journal article
- Language
- en
- Open access
- bronze
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