Glycogen synthase kinase-3 beta, sf9 Human Recombinant
Glycogen synthase kinase-3 beta Human Recombinant
Glycogen synthase kinase (GSK) is a serine/threonine protein kinase that mediates the addition of phosphate molecules onto serine and threonine amino acid residues . It was first discovered in 1980 as a regulatory kinase for glycogen synthase . In mammals, GSK exists in two isozymes encoded by two homologous genes: GSK-3α (GSK3A) and GSK-3β (GSK3B) . These isozymes are involved in various cellular processes and have been implicated in numerous diseases .
GSK-3 is a multifunctional enzyme that phosphorylates over 100 different proteins . It is ubiquitously expressed in various tissues, including the brain, liver, and muscles . GSK-3 is active in resting cells and is inhibited by several hormones such as insulin, endothelial growth factor, and platelet-derived growth factor . The enzyme plays a crucial role in glycogen metabolism, cell signaling, cellular transport, and other biological activities .
GSK-3 is involved in a wide range of biological functions. It regulates glycogen metabolism by phosphorylating and inactivating glycogen synthase . Additionally, GSK-3 plays a role in cell cycle control, apoptosis, embryonic development, cell differentiation, cell motility, microtubule function, cell adhesion, and inflammation . It is also implicated in the regulation of immune responses and pathogen recognition .
GSK-3 functions by phosphorylating serine or threonine residues on its target substrates . The enzyme has a positively charged pocket adjacent to the active site that binds a “priming” phosphate group attached to a serine or threonine four residues C-terminal of the target phosphorylation site . This unique mode of substrate recognition allows GSK-3 to regulate various signaling pathways, including those involved in cell death and survival .
The activity of GSK-3 is tightly regulated by several mechanisms. It is inhibited by phosphorylation of specific serine residues (Ser21 in GSK-3α and Ser9 in GSK-3β) via the PI3K/Akt pathway . Additionally, GSK-3 activity is controlled by intracellular localization, interactions with binding proteins, and post-translational modifications . These regulatory mechanisms ensure precise control of GSK-3 activity in various cellular contexts .
GSK-3 has significant applications in biomedical research, diagnostic tools, and therapeutic strategies. Inhibitors of GSK-3 are being explored as potential treatments for various diseases, including type 2 diabetes, Alzheimer’s disease, inflammation, cancer, and bipolar disorder . The enzyme’s role in multiple signaling pathways makes it a promising target for drug discovery and development .
GSK-3 plays a vital role throughout the life cycle, from development to aging and disease. During embryonic development, GSK-3 is involved in cell differentiation and organogenesis . In adulthood, it regulates various cellular processes, including metabolism and immune responses . Dysregulation of GSK-3 activity is associated with several age-related diseases, such as Alzheimer’s disease and cancer . Understanding the role of GSK-3 in these processes is crucial for developing therapeutic strategies to combat these diseases .