A STAT3 palmitoylation cycle promotes TH17 differentiation and colitis

• Published in: Nature (London) Vol. 586; no. 7829; pp. 434 - 439
• Main Authors: Zhang, Mingming, Zhou, Lixing, Xu, Yuejie, Yang, Min, Xu, Yilai, Komaniecki, Garrison Paul, Kosciuk, Tatsiana, Chen, Xiao, Lu, Xuan, Zou, Xiaoping, Linder, Maurine E., Lin, Hening
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 15.10.2020; Nature Publishing Group
• Subjects: 14/19; 14/35; 38; 38/109; 38/70; 38/77; 631/250/256; 631/45/607/1172; 631/80/86; 631/92/458; 82; 82/29; 82/80; 96; Cell activation; Cell differentiation; Colitis; Cysteine; Differentiation (biology); Disease; Helper cells; Humanities and Social Sciences; Inflammatory bowel disease; Inflammatory bowel diseases; Intestine; Kinases; Lymphocytes T; multidisciplinary; Nuclei (cytology); Palmitoylation; Perturbation; Phosphorylation; Plasma; Post-translation; Proteins; Recruitment; Science; Science (multidisciplinary); Signaling; Signs and symptoms; Stat3 protein; Stimulators; Thioesterase

Cysteine palmitoylation (S-palmitoylation) is a reversible post-translational modification that is installed by the DHHC family of palmitoyltransferases and is reversed by several acyl protein thioesterases 1 , 2 . Although thousands of human proteins are known to undergo S-palmitoylation, how this...