Heat shock cognate 71 (HSC71) regulates cellular antiviral response by impairing formation of VISA aggregates.
10.1007/s13238-013-3902-3
- Author:
Zhigang LIU
1
;
Shu-Wen WU
;
Cao-Qi LEI
;
Qian ZHOU
;
Shu LI
;
Hong-Bing SHU
;
Yan-Yi WANG
Author Information
1. College of Life Sciences, Wuhan University, Wuhan 430072, China.
- Publication Type:Journal Article
- MeSH:
Adaptor Proteins, Signal Transducing;
biosynthesis;
chemistry;
genetics;
metabolism;
Cell Aggregation;
genetics;
GPI-Linked Proteins;
metabolism;
Gene Knockdown Techniques;
HEK293 Cells;
HSC70 Heat-Shock Proteins;
genetics;
metabolism;
Heat-Shock Response;
genetics;
Humans;
Interferon Regulatory Factor-3;
genetics;
metabolism;
Interferon-beta;
genetics;
NF-kappa B;
genetics;
Prions;
metabolism;
Receptors, Retinoic Acid;
metabolism;
Viruses;
drug effects;
metabolism;
pathogenicity
- From:
Protein & Cell
2013;4(5):373-382
- CountryChina
- Language:English
-
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.
