The JAK-mediated phospho-tyrosine STAT1 is central for IFNs signaling and antiviral defense. However, the past research provide little insight on the potential STAT1 functionality in inflammatory responses.

The resarch group of Hozaifa Metwally and Tadamitsu Kishimoto (Immune Regulation, WPI-IFReC) uncoverd the first threonine phosphorylation of the transactivation domain of STAT1, and more generally other STAT proteins. They unveiled Thr748 as a conserved IFN-independent phosphorylation switch in Stat1, which restricts IFN signaling and promotes innate inflammatory responses following the recognition of the bacterial-derived toxin lipopolysaccharide (LPS).
(online publishing in Proceedings of the National Academy of Sciences USA (PNAS) on Apr. 15, 2024)

Figure: Threonine phosphorylation of STAT1 regulates the host's inflammatory responses.

Contact

Kang-Kishimoto Lab

kishimotoifrec.osaka-u.ac.jp

Immune Regulation