Per-Arnt-Sim Kinase (PASK)

Per-Arnt-Sim kinase (PASK) is a serine/threonine protein kinase that contains one or more PAS (Per-ARNT-Sim) domains at its N-terminus and a C-terminal catalytic kinase domain. It is the only known mammalian protein kinase to harbor a PAS domain, which acts as an environmental sensor for various physical and chemical stimuli. PASK functions primarily as a nutrient-responsive regulator involved in glucose metabolism, lipid metabolism, mitochondrial respiration, and regulation of gene expression. It plays key roles in pancreatic islet α/β cells affecting insulin secretion and blood glucose levels. PASK has been implicated in the control of pancreatic hormone release, insulin sensitivity regulation and protection against metabolic syndrome features such as obesity and hepatic steatosis. The endogenous physiological ligand(s) for the mammalian PASK PAS domains remain unidentified; however, phosphatidic acid and monophosphorylated phosphoinositides have been shown to bind and modulate its activity experimentally. PASK is evolutionarily conserved across eukaryotes.

Other names

PAS kinasePASKIN

PASK inhibitors (currently experimental) would act by inhibiting the kinase activity of PASK, potentially impacting glucose and lipid metabolism and insulin secretion.