DHHC17 Is a New Regulator of AMPK Signaling.

ABSTRACT: The association of AMP-activated protein kinase (AMPK) with membranes plays a critical role in the regulation of AMPK activation and function. Protein lipid modification, including palmitoylation, myristoylation, and farnesyation, constitutes a crucial mechanism in the regulation of protein dynamic interactions with membranes. Among the three subunits of the AMPK heterotrimeric complex, the structural subunit AMPKβ is myristoylated and the catalytic subunit AMPKα is palmitoylated. Here, we report the characterization of AMPKα palmitoylation. We found that AMKPα was palmitoylated at Cys209 and Cys543, and this was required for AMPK activation and subcellular membrane compartmentalization. To understand the regulation of AMPKα palmitoylation, we have identified DHHC17 as a candidate palmitoy

SUBMITTER: Sun Y 

PROVIDER: S-EPMC9387237 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature