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PASK phosphorylates and inactivates GSK3beta, thereby preventing PDX-1 (show PDX1 Proteins) serine phosphorylation and alleviating GSK3beta-mediated PDX-1 (show PDX1 Proteins) protein degradation in pancreatic beta-cells.
Mutations that affect PAS domain cause a severe protein trafficking defect and change the interactions with Kv11.1 (show KCNH2 Proteins) channels.
The role of PAS kinase in PASsing the glucose signal.
Per-Arnt (show ARNT Proteins)-Sim (show SIM2 Proteins) (PAS) domain-containing protein kinase (show CDK7 Proteins) (PASK) has a role in insulin (show INS Proteins) hypersecretion
PASK is involved in the regulation of glucagon (show GCG Proteins) secretion by glucose and may be a useful target for the treatment of type 2 diabetes.
Structural bases of PAS domain-regulated kinase (PASK) activation in the absence of activation loop phosphorylation.
Results suggest that elevated glucose concentrations rapidly increase Per-Arnt (show ARNT Proteins)-Sim (show SIM2 Proteins) kinase activity in pancreatic islet beta cells, followed by up-regulation by glucose of preproinsulin (show INS Proteins) and pancreatic duodenum homeobox (show Lbx1 Proteins) 1 gene expression.
identified the multifunctional eukaryotic translation elongation factor (show TSFM Proteins) eEF1A1 (show EEF1A1 Proteins) as a novel interaction partner of PASKIN in the nuclei of testis germ cells and in the midpiece of sperm tails
the PAS kinase function could be critical for preserving the nutrient effect on AMP-activated protein kinase (show PRKAA2 Proteins) and mammalian target of rapamycin (show FRAP1 Proteins)/S6K1 (show RPS6KB1 Proteins) pathways and maintain the regulatory role of exendin-4 in food intake
PASK is a key kinase in GLP-1 (show GCG Proteins) actions and exerts a coordinated response with the other metabolic sensors.
These data strongly suggest that PASK is required for normal nutrient partitioning and energy homeostasis in the mouse and that this activity is primarily carried out in a cell-autonomous fashion.[Review]
Targeted disruption of the PAS domain serine/threonine kinase was studied.
Paskin gene expression is not induced by glucose in pancreatic beta-cells and glucose-stimulated insulin (show INS Proteins) production is independent of PASKIN.
PASK acts in a cell-autonomous manner to maintain cellular energy homeostasis and is a potential therapeutic target for metabolic disease
Suggest that paskin is involved in the central control of hypoxic ventilation, modulating ventilation in a gender-dependent manner.
PASK is a novel mediator of glucolipotoxicity on the insulin (show INS Proteins) gene in pancreatic beta-cells
This gene encodes a member of the serine/threonine kinase family that contains two PAS domains. Expression of this gene is regulated by glucose, and the encoded protein plays a role in the regulation of insulin gene expression. Downregulation of this gene may play a role in type 2 diabetes. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
PAS domain-containing serine/threonine-protein kinase
, PAS domain containing serine/threonine kinase
, PAS domain-containing serine/threonine-protein kinase-like
, per-arnt-sim (PAS) domain kinase