Description
Product Characteristics:
PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.
Subcellular location: Cytoplasm, Nucleus
Synonyms: AMP activated protein kinase beta 2 non catalytic subunit, AMPK beta 2, AMPK beta 2 chain, PRKAB 2, Protein kinase AMP activated beta 2 non catalytic subunit, PRKAB1, AMPK subunit beta-1, AMPKb
Target Information: The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex. [provided by RefSeq, Jul 2008]