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The deubiquitinase CYLD is a specific checkpoint of the STING antiviral signaling pathway
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The deubiquitinase CYLD is a specific checkpoint of the STING antiviral signaling pathway
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Journal Article
The deubiquitinase CYLD is a specific checkpoint of the STING antiviral signaling pathway
2018
Overview
Stimulator of interferon genes (STING) is critical for cytosolic DNA-triggered innate immunity. STING is modified by several types of polyubiquitin chains. Here, we report that the deubiquitinase CYLD sustains STING signaling by stabilizing the STING protein. CYLD deficiency promoted the K48-linked polyubiquitination and degradation of STING, attenuating the induction of IRF3-responsive genes after HSV-1 infection or the transfection of DNA ligands. Additionally, CYLD knockout mice were more susceptible to HSV-1 infection than their wild-type (WT) littermates. Mechanistically, STING translocated from the ER to the Golgi upon HSV-1 stimulation; CYLD partially accumulated with STING and interacted selectively with K48-linked polyubiquitin chains on STING, specifically removing the K48-linked polyubiquitin chains from STING and ultimately boosting the innate antiviral response. Our study reveals that CYLD is a novel checkpoint in the cGAS-STING signaling pathway and sheds new light on the dynamic regulation of STING activity by ubiquitination.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Antiviral Agents - metabolism
/ Biological response modifiers
/ Biology
/ Cellular signal transduction
/ Chains
/ Cysteine Endopeptidases - metabolism
/ Deubiquitinating Enzyme CYLD - metabolism
/ DNA
/ Genes
/ Golgi Apparatus - metabolism
/ Herpesvirus 1, Human - metabolism
/ Humans
/ Immunity
/ Interferon regulatory factor 3
/ Kinases
/ Medicine and Health Sciences
/ Membrane Proteins - metabolism
/ Mice
/ Novels
