Literature summary for 2.7.7.86 extracted from

Xia, P.; Ye, B.; Wang, S.; Zhu, X.; Du, Y.; Xiong, Z.; Tian, Y.; Fan, Z.
Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity (2016), Nat. Immunol., 17, 369-378.

Search for more literature for 2.7.7.86

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q8C6L5	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	glutamylation and deglutamylation of cGAS tightly modulate immune responses to infection with DNA viruses. Polyglutamylation of cGAS by the enzyme TTLL6 impeded its DNA-binding ability, whereas TTLL4-mediated monoglutamylation of cGAS blocks its synthase activity. Conversely, carboxypeptidase CCP6 removes the polyglutamylation of cGAS, whereas CCP5 hydrolyzes the monoglutamylation of cGAS, which together lead to the activation of cGAS	Mus musculus

General Information

General Information	Comment	Organism
physiological function	glutamylation and deglutamylation of cGAS tightly modulate immune responses to infection with DNA viruses. Polyglutamylation of cGAS by the enzyme TTLL6 impeded its DNA-binding ability, whereas TTLL4-mediated monoglutamylation of cGAS blocks its synthase activity. Conversely, carboxypeptidase CCP6 removes the polyglutamylation of cGAS, whereas CCP5 hydrolyzes the monoglutamylation of cGAS, which together lead to the activation of cGAS	Mus musculus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)