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Modulation of YY1 activity by SAP30 总被引:3,自引:0,他引:3
Huang NE Lin CH Lin YS Yu WC 《Biochemical and biophysical research communications》2003,306(1):267-275
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Jie-lin Tang Qi Yang Chong-hui Xu He Zhao Ya-ling Liu Can-yu Liu Yuan Zhou Dong-wei Gai Rong-juan Pei Yun Wang Xue Hu Bo Zhong Yan-yi Wang Xin-wen Chen Ji-zheng Chen 《蛋白质与细胞》2021,12(4):261-278
TANK-binding kinase 1 (TBK1),a core kinase of antiviral pathways,activates the production of interferons (IFNs).It has been reported that deacetylation activates TBK1;however,the precise mechanism still remains to be uncovered.We show here that during the early stage of viral infection,the acetylatlon of TBK1 was increased,and the acetylation of TBK1 at Lys241 enhanced the recruitment of IRF3 to TBK1.HDAC3 directly deacety-lated TBK1 at Lys241 and Lys692,which resulted in the activation of TBK1.Deacetylation at Lys241 and Lys692 was critical for the kinase activity and dimerizatlon of TBK1 respectively.Using knockout cell lines and transgenic mice,we confirmed that a HDAC3 null mutant exhibited enhanced susceptibility to viral challenge via impaired productlon of type I IFNs.Furthermore,activated TBK1 phosphorylated HDAC3,which promoted the deacetylation activity of HDAC3 and formed a feedback loop.In this study,we illustrated the roles the acetylated and deacetylated forms of TBK1 play in antivlral innate responses and clarified the post-translational modulations involved in the interaction between TBK1 and HDAC3. 相似文献