PLK1 Protein, Mouse (Active, sf9, His)

PLK1, a serine/threonine-protein kinase, plays a pivotal role in orchestrating various essential functions throughout the M phase of the cell cycle. It regulates centrosome maturation and spindle assembly, facilitates the removal of cohesins from chromosome arms, inactivates anaphase-promoting complex/cyclosome (APC/C) inhibitors, and governs mitotic exit and cytokinesis. Operating by binding and phosphorylating proteins that are already phosphorylated on specific motifs recognized by the POLO box domains, PLK1 phosphorylates an extensive array of substrates, including BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1, HNRNPU, and others. PLK1's crucial roles include promoting centrosome functions and bipolar spindle assembly through the phosphorylation of KIZ, NEDD1, and NINL. Additionally, it governs mitotic exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1, and RACGAP1. PLK1's involvement extends to kinetochore functions, sister chromatid cohesion, and the regulation of various checkpoint proteins, positioning it as a key player in the intricate network governing cell cycle progression.