CDK1 Protein, Mouse (sf9, His-GST)

CDK1 Protein plays a central role in controlling the eukaryotic cell cycle by modulating both the centrosome cycle and mitotic onset. It facilitates the G2-M transition by associating with multiple interphase cyclins and phosphorylates an extensive array of substrates involved in diverse cellular processes, including cell cycle regulation, DNA repair, and apoptosis. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes, triggering centrosome separation, Golgi dynamics, nuclear envelope breakdown, and chromosome condensation. Upon successful alignment of chromosomes at the metaphase plate, CDK1 activity is turned off by WEE1- and PKMYT1-mediated phosphorylation, allowing sister chromatid separation, chromosome decondensation, nuclear envelope reformation, and cytokinesis. CDK1 also plays a role in cellular responses to DNA damage, as it is inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation, contributing to the G2 checkpoint. Reactivation after DNA repair occurs through WIP1-dependent signaling, leading to CDC25A/B/C-mediated dephosphorylation and the resumption of cell cycle progression. Additionally, CDK1 phosphorylates various substrates involved in microtubule dynamics, spindle formation, and cell survival, highlighting its multifaceted regulatory role in orchestrating essential cellular events.