PRKAB1 encodes the non-catalytic beta-1 regulatory subunit of AMP-activated protein kinase (AMPK), a critical cellular energy sensor. PRKAB1 functions as a scaffold protein that assembles the AMPK complex by bridging the catalytic alpha subunits and regulatory gamma subunits, enabling AMPK's core metabolic functions 1. Upon detection of reduced intracellular ATP, AMPK phosphorylates metabolic enzymes and transcription factors to activate energy-producing pathways while inhibiting energy-consuming biosynthetic processes and cell proliferation. PRKAB1 also facilitates cytoskeletal remodeling through myosin regulation and controls mitochondrial dynamics during cell migration 2. Recent studies reveal tissue-specific and isoform-specific roles: PRKAB1 exhibits differential functions compared to PRKAB2 in cardiac lineage specification of stem cells, with PRKAB1 affecting late-stage cardiomyocyte maturation 3. PRKAB1 demonstrates therapeutic relevance in metabolic diseases; buddleoside ameliorates nonalcoholic steatohepatitis (NASH) by directly binding PRKAB1 residues (Val81, Arg83, Ser108) and activating AMPK to enhance autophagy 1, while schisanhenol improves nonalcoholic fatty liver disease through miR-802/PRKAB1-mediated AMPK pathway activation 4. Additionally, PRKAB1 participates in inflammatory bowel disease pathogenesis through host-microbiota interactions 5, and metformin-induced sarcopenia involves PRKAB1 as a drug target 6. These findings establish PRKAB1 as a multifunctional metabolic hub with significant therapeutic potential.