| 研究実績の概要 |
Signal transducer and activator of transcription 1 (STAT1) regulates a wide-range of biological processes. Tyr701 phosphorylation of STAT1 signaling cascade is well known for its essential role in mediating cellular responses to interferons (IFN) such as antiviral response. However, Tyr701 phosphorylation cannot explain the full spectrum of STAT1 activities, especially in the context of bacterial infections and inflammation. Our study unraveled an endosomal-originated noncanonical signaling resulting in a noncanonical Thr749 phosphorylation, which confers STAT1 with distinct DNA binding and proinflammatory gene-regulatory properties in response to TLR4 stimulation. Our findings adds a dynamic dimension to the current working paradigm of STAT1 that may apply to other STAT family proteins.
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