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PP2A55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.

PLoS Genet.. 2014; 
HégaratNadia,VeselyClare,VinodP K,OcasioCory,PeterNisha,GannonJulian,OliverAntony W,NovákBéla,HocheggerHel
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Custom Vector Construction Fcp1 cDNA was synthesized by Genscript and cloned into the EGFP-C1 vector via Bgl2 and EcoR1 sites. Get A Quote

摘要

Entry into mitosis is triggered by activation of Cdk1 and inactivation of its counteracting phosphatase PP2A55. Greatwall kinase inactivates PP2A55 via its substrates Ensa and ARPP19. Both Greatwall and Ensa/ARPP19 are regulated by phosphorylation, but the dynamic regulation of Greatwall activity and the phosphatases that control Greatwall kinase and its substrates are poorly understood. To address these questions we applied a combination of mathematical modelling and experiments using phospho-specific antibodies to monitor Greatwall, Ensa/ARPP19 and Cdk substrate phosphorylation during mitotic entry and exit. We demonstrate that PP2A55 is required for Gwl dephosphorylation at the essential Cdk site Thr194.... More

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