AGR2-mediated cell-cell communication controls the antiviral immune response by promoting the thiol oxidation of TRAF3

• Published in: Redox biology Vol. 82; p. 103581
• Main Authors: Jia, Mengqi, Chen, Xiaojing, Guo, Wenxue, Ma, Dapeng, Wang, Peng, Niu, Huanmin, Liu, Changhong, Lin, Xianjuan, Lu, QiQi, Wang, Jing, Zheng, Xiaoxue, Sun, Qi, Gao, Chengjiang, Yuan, Huiqing
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.05.2025; Elsevier
• Subjects: AGR2; Animals; Disulfide bond; HEK293 Cells; Humans; Interferon Type I - metabolism; Macrophages - immunology; Macrophages - metabolism; Mice; Mucoproteins - genetics; Mucoproteins - metabolism; Oncogene Proteins - genetics; Oncogene Proteins - metabolism; Oxidation-Reduction; Protein disulfide isomerases; Research Paper; Sulfhydryl Compounds - metabolism; TNF Receptor-Associated Factor 3 - chemistry; TNF Receptor-Associated Factor 3 - genetics; TNF Receptor-Associated Factor 3 - metabolism; TRAF3; Type I interferon; AGR2; Type I interferon; Disulfide bond; TRAF3; Protein disulfide isomerases

Protein disulfide isomerases (PDIs) are essential catalysts for the formation and isomerization of disulfide bonds in diverse substrate proteins and exert multiple functions under pathophysiological conditions. Here, we show that anterior gradient 2 (AGR2), a member of PDIs, acts as a negative regul...