Protein Serine Threonine Kinases (PSTKs) are a class of enzymes that play a crucial role in regulating various biological processes within cells. They are a subset of the larger protein kinase family, which includes kinases that phosphorylate proteins on serine, threonine, or tyrosine residues. However, PSTKs specifically target and phosphorylate serine and threonine residues on target proteins.
PSTKs act as important signaling molecules within cellular pathways, facilitating communication between different cellular components and coordinating a wide range of cellular functions. By adding phosphate groups to specific serine and threonine residues, PSTKs modulate the activity and function of target proteins, thereby regulating processes such as cell growth, metabolism, proliferation, differentiation, and apoptosis.
The diverse roles and functions of PSTKs are achieved by their ability to phosphorylate multiple substrates, including transcription factors, enzymes, ion channels, and structural proteins. This versatility allows PSTKs to participate in various cellular processes, playing crucial roles in signal transduction, gene expression, and protein regulation.
PSTKs are involved in numerous cellular signaling pathways, including those mediated by growth factors, hormones, and stress triggers. Dysregulation or mutations in PSTK genes have been implicated in various diseases, including cancers, neurodegenerative disorders, and metabolic disorders. Thus, understanding the mechanisms and functions of PSTKs is vital for unraveling cellular processes and designing therapeutic interventions for diseases associated with aberrant kinase signaling.
