Source

Rabbit

Reactivity

Human;Mouse;Rat

Background

PASK is a serine/threonine kinase that contains two PAS domains. Its kinase activity is up-regulated by autophosphorylation of the activation loop within its catalytic domain and is inhibited in cis by one of the PAS domains. Studies found that the yeast homolog of PASK phosphorylates and inhibits two enzymes required for glycogen biosynthesis: UDP-glucose pyrophosphorylase and glycogen synthase, resulting in the decrease of carbohydrate storage. Further studies showed that increased glucose levels activate PASK activity and enhance its expression in pancreatic β-cells. PASK is essential for the glucose-stimulated expression of preproinsulin and Pdx1, suggesting its role in the regulation of genes involved in pancreatic β-cell functions. PASK was shown to be critical for glucose-stimulated insulin secretion in pancreatic β-cells. The absence of PASK also protects animals from obesity and insulin resistance when they are fed a high-fat diet. These findings suggest that PASK functions as an important metabolic sensor in various cells.

References

[1] Rutter, J. et al. (2001) Proc Natl Acad Sci USA 98, 8991-6.
[2] Rutter, J. et al. (2002) Cell 111, 17-28.
[3] da Silva Xavier, G. et al. (2004) Proc Natl Acad Sci USA 101, 8319-24.
[4] Hao, H.X. et al. (2007) Proc Natl Acad Sci USA 104, 15466-71.

Raw materials

Preparation Products