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• W4387579076 abstract "The translocation of stimulator of interferon genes (STING) from the endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) enables its activation. However, the mechanism underlying the regulation of STING exit from the ER remains elusive. Here, we found that STING induces the activation of transforming growth factor beta-activated kinase 1 (TAK1) prior to STING trafficking in a TAK1 binding protein 1 (TAB1)-dependent manner. Intriguingly, activated TAK1 directly mediates STING phosphorylation on serine 355, which facilitates its interaction with STING ER exit protein (STEEP) and thereby promotes its oligomerization and translocation to the ERGIC for subsequent activation. Importantly, activation of TAK1 by monophosphoryl lipid A, a TLR4 agonist, boosts cGAMP-induced antitumor immunity dependent on STING phosphorylation in a mouse allograft tumor model. Taken together, TAK1 was identified as a checkpoint for STING activation by promoting its trafficking, providing a basis for combinatory tumor immunotherapy and intervention in STING-related diseases." @default.
• W4387579076 created "2023-10-13" @default.
• W4387579076 creator A5004498551 @default.
• W4387579076 creator A5028025664 @default.
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• W4387579076 creator A5086529957 @default.
• W4387579076 creator A5089051100 @default.
• W4387579076 date "2023-10-01" @default.
• W4387579076 modified "2023-10-17" @default.
• W4387579076 title "TAK1 is an essential kinase for STING trafficking" @default.
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