Plk, or Polo-like kinase, is a pivotal regulator of cell cycle progression and cellular proliferation, crucial for maintaining genomic stability and ensuring accurate cell division. Its multifaceted role encompasses the coordination of key processes such as centrosome maturation, spindle assembly, chromosome segregation, and cytokinesis. Dysregulation of Plk activity has been implicated in various pathological conditions, including cancer, where aberrant Plk expression or function can contribute to uncontrolled cell growth and tumor progression.
Inhibition of Plk activity offers a promising avenue for understanding cellular processes with dysregulated cell division. Various strategies have been devised to inhibit Plk function, including the development of small molecule inhibitors and peptide-based approaches. These inhibitors typically target critical domains of Plk involved in catalytic activity or protein-protein interactions, effectively disrupting its ability to phosphorylate substrates and execute its regulatory functions. By elucidating the mechanisms of Plk inhibition, researchers aim to gain insights into fundamental cellular processes.