A STAT3 palmitoylation cycle promotes T_H17 differentiation and colitis.

ABSTRACT: 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 modification is regulated to modulate specific biological functions is poorly understood. Here we report that the key T helper 17 (T_H17) cell differentiation stimulator, STAT3^3,4, is subject to reversible S-palmitoylation on cysteine 108. DHHC7 palmitoylates STAT3 and promotes its membrane recruitment and phosphorylation. Acyl protein thioesterase 2 (APT2, also known as LYPLA2) depalmitoylates phosphorylated STAT3 (p-STAT3) and enables it to translocate to the nucleu

SUBMITTER: Zhang M 

PROVIDER: S-EPMC7874492 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature