Heat shock cognate 71 (HSC71) regulates cellular antiviral response by impairing formation of VISA aggregates
Protein & Cell
;
(12): 373-382, 2013.
Article
in English
| WPRIM
| ID: wpr-757799
ABSTRACT
In response to viral infection, RIG-I-like RNA helicases detect viral RNA and signal through the mitochondrial adapter protein VISA. VISA activation leads to rapid activation of transcription factors IRF3 and NF-κB, which collaborate to induce transcription of type I interferon (IFN) genes and cellular antiviral response. It has been demonstrated that VISA is activated by forming prion-like aggregates. However, how this process is regulated remains unknown. Here we show that overexpression of HSC71 resulted in potent inhibition of virus-triggered transcription of IFNB1 gene and cellular antiviral response. Consistently, knockdown of HSC71 had opposite effects. HSC71 interacted with VISA, and negatively regulated virus-triggered VISA aggregation. These findings suggest that HSC71 functions as a check against VISA-mediated antiviral response.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Virulence
/
Viruses
/
Prions
/
Cell Aggregation
/
Chemistry
/
NF-kappa B
/
Interferon-beta
/
Receptors, Retinoic Acid
/
Heat-Shock Response
/
Adaptor Proteins, Signal Transducing
Limits:
Humans
Language:
English
Journal:
Protein & Cell
Year:
2013
Type:
Article
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