PRKAG1
Description
The PRKAG1 (protein kinase AMP-activated non-catalytic subunit gamma 1) is a protein-coding gene located on chromosome 12.
PRKAG1 encodes a regulatory subunit of AMP-activated protein kinase (AMPK). AMPK is a heterotrimer composed of a catalytic alpha subunit and non-catalytic beta and gamma subunits. AMPK is a vital energy-sensing enzyme that monitors cellular energy levels. In response to metabolic stress, AMPK activates, phosphorylating and inactivating key enzymes like acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), involved in fatty acid and cholesterol synthesis. PRKAG1 is one of the gamma regulatory subunits of AMPK. Multiple transcript variants encoding distinct isoforms have been observed. PRKAG1 has been shown to interact with PRKAB2 and PRKAB1.
PRKAG1 encodes a non-catalytic subunit of AMP-activated protein kinase (AMPK), a crucial energy sensor that regulates cellular energy metabolism. AMPK responds to decreased intracellular ATP levels by stimulating energy-producing pathways and inhibiting energy-consuming processes, including protein, carbohydrate, and lipid biosynthesis, as well as cell growth and proliferation. This occurs through direct phosphorylation of metabolic enzymes and longer-term effects mediated by phosphorylation of transcription regulators. PRKAG1, as part of the AMPK complex, also regulates cellular polarity by remodeling the actin cytoskeleton, potentially via indirect activation of myosin. PRKAG1 directly binds AMP, ADP, and ATP, which in turn activate or inhibit AMPK. AMP binding allosterically activates the alpha catalytic subunit of AMPK (PRKAA1 or PRKAA2) by inducing phosphorylation and preventing dephosphorylation. ADP similarly stimulates phosphorylation, while ATP promotes dephosphorylation, rendering the AMPK inactive.
PRKAG1 is also known as AMPKG.
