Structural basis of STING binding with and phosphorylation by TBK1.

ABSTRACT: The invasion of mammalian cytoplasm by microbial DNA from infectious pathogens or by self DNA from the nucleus or mitochondria represents a danger signal that alerts the host immune system¹. Cyclic GMP-AMP synthase (cGAS) is a sensor of cytoplasmic DNA that activates the type-I interferon pathway². On binding to DNA, cGAS is activated to catalyse the synthesis of cyclic GMP-AMP (cGAMP) from GTP and ATP³. cGAMP functions as a second messenger that binds to and activates stimulator of interferon genes (STING)^3-9. STING then recruits and activates tank-binding kinase 1 (TBK1), which phosphorylates STING and the transcription factor IRF3 to induce type-I interferons and other cytokines^10,11. However, how cGAMP-bound STING activates TBK1 an

SUBMITTER: Zhang C 

PROVIDER: S-EPMC6862768 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature