Protein phosphatase PP2Cα S-glutathionylation regulates cell migration.

ABSTRACT: Redox signaling is a fundamental mechanism that controls all major biological processes partly via protein cysteine oxidations, including S-glutathionylation. Despite over 2000 cysteines identified to form S-glutathionylation in databases, the identification of redox cysteines functionally linked to a biological process of interest remains challenging. Here, we demonstrate a strategy combining glutathionylation proteomic database, bioinformatics, and biological screening, which resulted in the identification of S-glutathionylated proteins, including PP2Cα, as redox players of cell migration. We showed that PP2Cα, a prototypical magnesium-dependent serine/threonine phosphatase, is susceptible to S-glutathionylation selectively at nonconserved C314. PP2Cα glutathionylation causes increased m

SUBMITTER: Kukulage DSK 

PROVIDER: S-EPMC11530597 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature