5'-AMP-activated protein kinase subunit beta-1 (PRKAB1) (PRKAB1)

PRKAB1 (5'-AMP-activated protein kinase subunit beta-1) is a regulatory subunit of the AMP-activated protein kinase (AMPK) heterotrimer, a critical energy-sensing enzyme that maintains cellular energy homeostasis [1, 2, 8]. AMPK is activated under conditions of metabolic stress, such as hypoxia or nutrient deprivation, which increase the cellular AMP/ATP ratio [4, 10]. Once activated, the AMPK complex promotes energy-producing catabolic pathways, such as fatty acid oxidation and glucose uptake, while inhibiting energy-consuming anabolic processes like lipid and protein synthesis [2, 11]. PRKAB1 serves as a scaffold for the assembly of the alpha and gamma subunits and contains a carbohydrate-binding module that facilitates interaction with glycogen [5, 8]. Therapeutic targeting of PRKAB1-containing complexes is a key strategy for treating metabolic disorders like type 2 diabetes and obesity, as well as exploring potential applications in cancer and neurodegeneration [3, 6, 14]. Drugs such as metformin and specific allosteric activators like A-769662 leverage this pathway to restore metabolic balance and improve insulin sensitivity [10, 11, 12].

Other names

AMPK beta-1 [2, 8]HAMPKb [2, 8]AMPKb [2, 8]5'-AMP-activated protein kinase beta-1 subunit [2, 8]Protein kinase AMP-activated non-catalytic subunit beta 1 [2, 4]

Allosteric activation of the AMPK heterotrimer and stabilization of the active conformation, facilitating phosphorylation of the catalytic alpha subunit at Thr172 by upstream kinases like LKB1 [6, 10, 11].