PASK/STK37

PASK/STK37 (also known as STK37 or PAS kinase) is a nutrient- and energy-sensing serine/threonine kinase belonging to the PAS-domain kinase family. Substrates phosphorylated by PASK/STK37 include PDX1, Wdr5, eEF1A1, and glycogen synthase; through these interactions, it regulates insulin transcription, protein translation, and glycogen and lipid synthesis. PASK/STK37 influences glucose-stimulated insulin secretion in β-cells, lipid metabolism in hepatocytes, fatty acid oxidation in skeletal muscle, as well as metabolic reprogramming and the maintenance of stemness in tumor cells. Within metabolic pathways, PASK/STK37 engages in cross-regulation with AMPK, mTOR/S6K, and nutrient signaling pathways; additionally, it can impact gene transcription through Wdr5-mediated epigenetic regulation. Given its pivotal role in glucose and lipid metabolism, β-cell function, tumor metabolism, and stem cell fate determination, PASK/STK37 has emerged as a critical research target in the fields of metabolic diseases, cancer therapeutics, and regenerative medicine.