Protein Kinase, AMP-Activated, Beta 1 Non-Catalytic Subunit, also known as PRKAB1, is a regulatory subunit of the AMP-activated protein kinase (AMPK) complex. AMPK is a crucial energy-sensing enzyme that monitors cellular energy status and plays a significant role in maintaining energy homeostasis. The AMPK complex is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits .
The PRKAB1 gene encodes the beta-1 subunit of the AMPK complex. This subunit is non-catalytic but is essential for the proper functioning of the AMPK enzyme. The AMPK complex is activated in response to cellular metabolic stresses, such as low glucose levels, hypoxia, and exercise. Upon activation, AMPK phosphorylates and inactivates key enzymes involved in regulating de novo biosynthesis of fatty acids and cholesterol, such as acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR) .
AMPK acts as a metabolic master switch, regulating several intracellular systems, including the uptake of glucose, the oxidation of fatty acids, and the biogenesis of mitochondria. The beta-1 subunit, encoded by PRKAB1, is believed to be a positive regulator of AMPK activity. Myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK .
The PRKAB1 gene is located on chromosome 12 in humans. It has several aliases, including AMPK subunit beta-1, AMPK beta 1, and 5’-AMP-activated protein kinase subunit beta-1 . The gene is expressed in various tissues, with high expression levels in the rectum, kidney, body of the stomach, spleen, renal medulla, upper lobe of the left lung, body of the pancreas, right lung, minor salivary glands, and left adrenal gland .