Release date: 2008-09-17
A recent study by researchers at the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences found that Î²-arrestin1 mediates the key transcription factor STAT1 and its negative in the interferon gamma (IFN-Î³) pathway. The interaction of the regulatory factor phosphatase TC45, which negatively regulates the response of cells to interferon gamma stimulation, inhibits the antiviral effect of interferon gamma. Experts stressed: "This study found a new function of Î²-arrestin1 protein in the nucleus and revealed a negative regulatory mechanism of STAT1 protein in the nucleus."
Interferon gamma is a cytokine with important physiological functions such as antiviral, antiproliferative, and immune regulation in the body. When the body is subjected to viral infection, interferon can activate the JAK-STAT1 pathway in the body, causing tyrosine phosphorylation, nuclear entry, activation of transcription of the interferon-responsive gene, and anti-viral functions.
Researchers Mo Yan and Zhang Liang found that Î²-arrestin1 interacts with STAT1 nucleus under interferon gamma stimulation, and accelerates STAT1 by recruiting tyrosine phosphatase TC45 to STAT1. Phosphorylation, down-regulation of interferon gamma signal, inhibits its antiviral activity. As the most important transcription factor in the interferon gamma pathway, STAT1 plays an important role in antiviral infection, anti-proliferation and immune regulation by regulating gene transcription. The over-activation of STAT1 is closely related to tumor formation and hematopoietic cell disorder. Intranuclear tyrosine dephosphorylation is considered to be the most important negative regulator of STAT1. The findings of this study contribute to a deeper understanding of the STAT1 negative regulator, and the discovery of new functions in the beta-arrestin1 nucleus has implications for understanding the importance of intranuclear distribution.
Source: China Medicine 123 Network
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