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Details on Person Endogenous STAT6 was found to co-fractionate with STING from...

Class:IdSummation:3249363
_displayNameEndogenous STAT6 was found to co-fractionate with STING from...
_timestamp2013-04-11 15:38:05
created[InstanceEdit:3249364] Shamovsky, V, 2013-04-09
literatureReference[LiteratureReference:3249356] Activation of STAT6 by STING is critical for antiviral innate immunity
[LiteratureReference:2395975] Structural Analysis of the STING Adaptor Protein Reveals a Hydrophobic Dimer Interface and Mode of Cyclic di-GMP Binding
modified[InstanceEdit:3261243] Shamovsky, V, 2013-04-10
[InstanceEdit:3270621] Shamovsky, V, 2013-04-11
textEndogenous STAT6 was found to co-fractionate with STING from the lysates of Herpes simplex virus 1 (HSV-1) - infected HeLa cells. Similar results were obtained from Sendai virus (SeV)-infected HeLa cells, where STAT6 redistributed to the perinuclear region to co-localizes with STING upon infection. Co-immunoprecipitation assays confirmed STAT6-STING interaction in human embryonic kidney HEK293 cells. The DNA-binding domain (DBD) of STAT6 and C terminus (aa 317-379) of STING were essential for this interaction. The TBK1 kinase activity was required for virus-induced STAT6 phosphorylation, however the direct interaction between STAT6 and TBK1 is not yet reported (Chen H et al. 2011). Co-immunoprecipitation assays in HEK293T cells expressing HA-tagged STING and Flag-tagged TBK1 showed that TBK directly interacts with STING (Ouyang S et al. 2012).
(summation)[Reaction:3249378] STING recruits TBK1 and STAT6 [Homo sapiens]
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