西亚试剂：Nuclear β-Arrestin1 Functions as a Scaffold for the Dephosp

Molecular Cell, Vol 31, 695-707, 05 September 2008

Nuclear β-Arrestin1 Functions as a Scaffold for the Dephosphorylation of STAT1 and Moderates the Antiviral Activity of IFN-γ

Wei Mo,1,5 Liang Zhang,1,5 Guohua Yang,1 Jianwei Zhai,1 Zhonghua Hu,1 Yuelei Chen,1Xu Chen,2 Lijian Hui,3 Ruimin Huang,4 and Gengxi Hu1,

1 State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China
2 Department of Ophthalmology, Zhongshan Hospital, Fudan University, Shanghai 200032, China
3 Research Institute of Molecular Pathology, A-1030 Vienna, Austria
4 Department of Neurology, Molecular Pharmacology and Chemistry Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, NY 10065, USA

Corresponding author
Gengxi Hu
Signal transducers and activators of transcription 1 (STAT1) is activated by tyrosine phosphorylation upon interferon-γ (IFN-γ) stimulation. Phosphorylated STAT1 translocates into nucleus to initiate the transcription of IFN-γ target genes that are important in mediating antiviral, antiproliferative, and immune response. The inactivation of STAT1 is mainly accomplished via tyrosine dephosphorylation by the nuclear isoform of T cell protein tyrosine phosphatase (TC45) in nucleus. Here we show that β-arrestin1 directly interacts with STAT1 in nucleus after IFN-γ treatment and accelerates STAT1 tyrosine dephosphorylation by recruiting TC45. Consequently, β-arrestin1 negatively regulates STAT1 transcription activity as well as the IFN-γ-induced gene transcription. Application of β-arrestin1 siRNA significantly enhances IFN-γ-induced antiviral response in vesicular stomatitis virus (VSV)-infected cells. Our results reveal that nuclear β-arrestin1, acting as a scaffold for the dephosphorylation of STAT1, is an essential negative regulator of IFN-γ signaling and participates in the IFN-γ-induced cellular antiviral response.

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