Schmitz, M. H. A. et al. Live-cell imaging RNAi screen identifies PP2A–B55α and importin-β1 as key mitotic exit regulators in human cells. Nat. Cell Biol. 12, 886–893 (2010).
Mochida, S., Ikeo, S., Gannon, J. & Hunt, T. Regulated activity of PP2A–B55 δ is crucial for controlling entry into and exit from mitosis in Xenopus egg extracts. EMBO J. 28, 2777–2785 (2009).
Manchado, E. et al. Targeting mitotic exit leads to tumor regression in vivo: modulation by Cdk1, Mastl, and the PP2A/B55α,δ phosphatase. Cancer Cell 18, 641–654 (2010).
Agostinis, P., Derua, R., Sarno, S., Goris, J. & Merlevede, W. Specificity of the polycation-stimulated (type-2A) and ATP, Mg-dependent (type-1) protein phosphatases toward substrates phosphorylated by P34cdc2 kinase. Eur. J. Biochem. 205, 241–248 (1992).
Mayer-Jaekel, R. E. et al. The 55 kd regulatory subunit of Drosophila protein phosphatase 2A is required for anaphase. Cell 72, 621–633 (1993).
Suzuki, K. et al. Identification of non-Ser/Thr-Pro consensus motifs for Cdk1 and their roles in mitotic regulation of C2H2 zinc finger proteins and Ect2. Sci. Rep. 5, 7929 (2015).
Chen, C. et al. Identification of a major determinant for serine-threonine kinase phosphoacceptor specificity. Mol. Cell 53, 140–147 (2014).
Pinna, L. A., Donella, A., Clari, G. & Moret, V. Preferential dephosphorylation of protein bound phosphorylthreonine and phosphorylserine residues by cytosol and mitochondrial “casein phosphatases”. Biochem. Biophys. Res. Commun. 70, 1308–1315 (1976).
Deana, A. D., Marchiori, F., Meggio, F. & Pinna, L. A. Dephosphorylation of synthetic phosphopeptides by protein phosphatase-T, a phosphothreonyl protein phosphatase. J. Biol. Chem. 257, 8565–8568 (1982).
Deana, A. D. & Pinna, L. A. Identification of pseudo ‘phosphothreonyl-specific’ protein phosphatase T with a fraction of polycation-stimulated protein phosphatase 2A. Biochim. Biophys. Acta 968, 179–185 (1988).
Cundell, M. J. et al. A PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit. J. Cell Biol. 214, 539–554 (2016).
McCloy, R. A. et al. Global phosphoproteomic mapping of early mitotic exit in human cells identifies novel substrate dephosphorylation motifs. Mol. Cell Proteomics 14, 2194–2212 (2015).
Malik, R. et al. Quantitative analysis of the human spindle phosphoproteome at distinct mitotic stages. J. Proteome Res. 8, 4553–4563 (2009).
Godfrey, M. et al. PP2A(Cdc55) phosphatase imposes ordered cell-cycle phosphorylation by opposing threonine phosphorylation. Mol. Cell 65, 393–402 (2017).
Pines, J. Cubism and the cell cycle: the many faces of the APC/C. Nat. Rev. Mol. Cell Biol. 12, 427–438 (2011).
Labit, H. et al. Dephosphorylation of Cdc20 is required for its C-box-dependent activation of the APC/C. EMBO J. 31, 3351–3362 (2012).
Yudkovsky, Y., Shteinberg, M., Listovsky, T., Brandeis, M. & Hershko, A. Phosphorylation of Cdc20/fizzy negatively regulates the mammalian cyclosome/APC in the mitotic checkpoint. Biochem. Biophys. Res. Commun. 271, 299–304 (2000).
Strickfaden, S. C. et al. A mechanism for cell-cycle regulation of MAP kinase signaling in a yeast differentiation pathway. Cell 128, 519–531 (2007).
Zhang, S. et al. Molecular mechanism of APC/C activation by mitotic phosphorylation. Nature 533, 260–264 (2016).
Fujimitsu, K., Grimaldi, M. & Yamano, H. Cyclin-dependent kinase 1-dependent activation of APC/C ubiquitin ligase. Science 352, 1121–1124 (2016).
Qiao, R. et al. Mechanism of APC/CCDC20 activation by mitotic phosphorylation. Proc. Natl Acad. Sci. USA 113, 2570–2578 (2016).
Hein, J. B. & Nilsson, J. Interphase APC/C-Cdc20 inhibition by cyclin A2–Cdk2 ensures efficient mitotic entry. Nat. Commun. 7, 10975 (2016).
Gharbi-Ayachi, A. et al. The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A. Science 330, 1673–1677 (2010).
Mochida, S., Maslen, S. L., Skehel, M. & Hunt, T. Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis. Science 330, 1670–1673 (2010).
Floyd, S., Pines, J. & Lindon, C. APC/C Cdh1 targets aurora kinase to control reorganization of the mitotic spindle at anaphase. Curr. Biol. 18, 1649–1658 (2008).
Chang, L., Zhang, Z., Yang, J., McLaughlin, S. H. & Barford, D. Atomic structure of the APC/C and its mechanism of protein ubiquitination. Nature 522, 450–454 (2015).
Kramer, E. R., Scheuringer, N., Podtelejnikov, A. V., Mann, M. & Peters, J. M. Mitotic regulation of the APC activator proteins CDC20 and CDH1. Mol. Biol. Cell 11, 1555–1569 (2000).
Zeng, X. et al. Pharmacologic inhibition of the anaphase-promoting complex induces a spindle checkpoint-dependent mitotic arrest in the absence of spindle damage. Cancer Cell 18, 382–395 (2010).
van der Horst, A. & Lens, S. M. A. Cell division: control of the chromosomal passenger complex in time and space. Chromosoma 123, 25–42 (2014).
Hümmer, S. & Mayer, T. U. Cdk1 negatively regulates midzone localization of the mitotic kinesin Mklp2 and the chromosomal passenger complex. Curr. Biol. 19, 607–612 (2009).
Goto, H. et al. Complex formation of Plk1 and INCENP required for metaphase–anaphase transition. Nat. Cell Biol. 8, 180–187 (2006).
Hertz, E. P. T. et al. A conserved motif provides binding specificity to the PP2A–B56 phosphatase. Mol. Cell 63, 686–695 (2016).
Bremmer, S. C. et al. Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine. J. Biol. Chem. 287, 1662–1669 (2012).
Kemp, B. E. Relative alkali stability of some peptide o-phosphoserine and o-phosphothreonine esters. FEBS Lett. 110, 308–312 (1980).
Donella Deana, A., Krinks, M. H., Ruzzene, M., Klee, C. & Pinna, L. A. Dephosphorylation of phosphopeptides by calcineurin (protein phosphatase 2B). Eur. J. Biochem. 219, 109–117 (1994).
Hein, J. B. & Nilsson, J. Stable MCC binding to the APC/C is required for a functional spindle assembly checkpoint. EMBO Rep. 15, 264–272 (2014).
Cundell, M. J. et al. The BEG (PP2A–B55/ENSA/Greatwall) pathway ensures cytokinesis follows chromosome separation. Mol. Cell 52, 393–405 (2013).
Sedgwick, G. G. et al. Mechanisms controlling the temporal degradation of Nek2A and Kif18A by the APC/C–Cdc20 complex. EMBO J. 32, 303–314 (2013).