A cell-free assay implicates a role of sphingomyelin and cholesterol in STING phosphorylation
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Title
A cell-free assay implicates a role of sphingomyelin and cholesterol in STING phosphorylation
Authors
Keywords
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Journal
Scientific Reports
Volume 11, Issue 1, Pages -
Publisher
Springer Science and Business Media LLC
Online
2021-06-07
DOI
10.1038/s41598-021-91562-z
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Related references
Note: Only part of the references are listed.- Homeostatic regulation of STING by retrograde membrane traffic to the ER
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- The binding of TBK1 to STING requires exocytic membrane traffic from the ER
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- Nitro-fatty acids are formed in response to virus infection and are potent inhibitors of STING palmitoylation and signaling
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- TMED2 Potentiates Cellular IFN Responses to DNA Viruses by Reinforcing MITA Dimerization and Facilitating Its Trafficking
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- Activation of STING requires palmitoylation at the Golgi
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- STING Activation by Translocation from the ER Is Associated with Infection and Autoinflammatory Disease
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- COPA mutations impair ER-Golgi transport and cause hereditary autoimmune-mediated lung disease and arthritis
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- Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs
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- ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization
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- MPYS, a Novel Membrane Tetraspanner, Is Associated with Major Histocompatibility Complex Class II and Mediates Transduction of Apoptotic Signals
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