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Publication : Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity.

First Author  Xia P Year  2016
Journal  Nat Immunol Volume  17
Issue  4 Pages  369-78
PubMed ID  26829768 Mgi Jnum  J:231311
Mgi Id  MGI:5770179 Doi  10.1038/ni.3356
Citation  Xia P, et al. (2016) Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity. Nat Immunol 17(4):369-78
abstractText  Cyclic GMP-AMP synthase (cGAS) senses cytosolic DNA during viral infection and catalyzes synthesis of the dinucleotide cGAMP, which activates the adaptor STING to initiate antiviral responses. Here we found that deficiency in the carboxypeptidase CCP5 or CCP6 led to susceptibility to DNA viruses. CCP5 and CCP6 were required for activation of the transcription factor IRF3 and interferons. Polyglutamylation of cGAS by the enzyme TTLL6 impeded its DNA-binding ability, whereas TTLL4-mediated monoglutamylation of cGAS blocked its synthase activity. Conversely, CCP6 removed the polyglutamylation of cGAS, whereas CCP5 hydrolyzed the monoglutamylation of cGAS, which together led to the activation of cGAS. Therefore, glutamylation and deglutamylation of cGAS tightly modulate immune responses to infection with DNA viruses.
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