PP2A function toward mitotic kinases and substrates during

• Main Authors: Ae Lee Jeong, Young Yang
• Format: Article
• Language: English
• Published: Korean Society for Biochemistry and Molecular Biology 2013-06-01
• Series: BMB Reports
• Subjects: Aurora B; CDK1:cyclin B; Cell cycle; PLK1; PP2A
• Online Access: http://bmbreports.org/jbmb/pdf.php?data=MTMwOTI3MThAcGRmX3JhaW50cmFjZV9sZWV5c0AlNUI0Ni02JTVEMTMwNjI1MjMwMV8lMjgyODktMjk0JTI5Qk1CXzEzLTA0MS5wZGY=

To maintain cellular homeostasis against the demands of theextracellular environment, a precise regulation of kinases andphosphatases is essential. In cell cycle regulation mechanisms,activation of the cyclin-dependent kinase (CDK1) and cyclin Bcomplex (CDK1:cyclin B) causes a remarkable change inprotein phosphorylation. Activation of CDK1:cyclin B isregulated by two auto-amplification loops-CDK1:cyclin B activatesCdc25, its own activating phosphatase, and inhibitsWee1, its own inhibiting kinase. Recent biological evidencehas revealed that the inhibition of its counteracting phosphataseactivity also occurs, and it is parallel to CDK1:cyclin B activationduring mitosis. Phosphatase regulation of mitotic kinasesand their substrates is essential to ensure that the progressionof the cell cycle is ordered. Outlining how the mutual controlof kinases and phosphatases governs the localization andtiming of cell division will give us a new understanding aboutcell cycle regulation. [BMB Reports 2013; 46(6): 289-294]