Unknown

Dataset Information

0

Heat shock cognate 71 (HSC71) regulates cellular antiviral response by impairing formation of VISA aggregates.


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-?B, 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.

SUBMITTER: Liu Z 

PROVIDER: S-EPMC4875550 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Heat shock cognate 71 (HSC71) regulates cellular antiviral response by impairing formation of VISA aggregates.

Liu Zhigang Z   Wu Shu-Wen SW   Lei Cao-Qi CQ   Zhou Qian Q   Li Shu S   Shu Hong-Bing HB   Wang Yan-Yi YY  

Protein & cell 20130430 5


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 HS  ...[more]

Similar Datasets

| S-EPMC2614971 | biostudies-literature
| S-EPMC7057768 | biostudies-literature
| S-EPMC1317673 | biostudies-literature
| S-EPMC8641652 | biostudies-literature
| S-EPMC8931677 | biostudies-literature
| S-EPMC1065288 | biostudies-literature
| S-EPMC1963456 | biostudies-literature
2022-02-15 | PXD028282 | Pride
| S-EPMC514856 | biostudies-literature
| S-EPMC5350560 | biostudies-literature