Wee1 and Cdc25 are controlled by conserved PP2A-dependent mechanisms in fission yeast

References

• Gould KL, Nurse P. Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature 1989; 342:39-45; PMID:2682257; http://dx.doi.org/10.1038/342039a0
   PubMed Web of Science ®Google Scholar
• Russell P, Nurse P. cdc25+ functions as an inducer in the mitotic control of fission yeast. Cell 1986; 45:145-53; PMID:3955656; http://dx.doi.org/10.1016/0092-8674(86)90546-5
   PubMed Web of Science ®Google Scholar
• Kumagai A, Dunphy WG. The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system. Cell 1991; 64:903-14; PMID:1825803; http://dx.doi.org/10.1016/0092-8674(91)90315-P
   PubMed Web of Science ®Google Scholar
• Gautier J, Solomon MJ, Booher RN, Bazan JF, Kirschner MW. cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2. Cell 1991; 67:197-211; PMID:1913817; http://dx.doi.org/10.1016/0092-8674(91)90583-K
   PubMed Web of Science ®Google Scholar
• Strausfeld U, Labbé JC, Fesquet D, Cavadore JC, Picard A, Sadhu K, Russell P, Dorée M. Dephosphorylation and activation of a p34cdc2/cyclin B complex in vitro by human CDC25 protein. Nature 1991; 351:242-5; PMID:1828290; http://dx.doi.org/10.1038/351242a0
   PubMed Web of Science ®Google Scholar
• Nurse P. Genetic control of cell size at cell division in yeast. Nature 1975; 256:547-51; PMID:1165770; http://dx.doi.org/10.1038/256547a0
   PubMed Web of Science ®Google Scholar
• Thuriaux P, Nurse P, Carter B. Mutants altered in the control co-ordinating cell division with cell growth in the fission yeast Schizosaccharomyces pombe. Mol Gen Genet 1978; 161:215-20; PMID:672898
   PubMedGoogle Scholar
• Fantes P, Nurse P. Control of cell size in fission yeast by a growth modulated size control over nuclear division. Exp Cell Res 1977; 107:377-86; PMID:872891; http://dx.doi.org/10.1016/0014-4827(77)90359-7
   PubMed Web of Science ®Google Scholar
• Harvey SL, Charlet A, Haas W, Gygi SP, Kellogg DR. Cdk1-dependent regulation of the mitotic inhibitor Wee1. Cell 2005; 122:407-20; PMID:16096060; http://dx.doi.org/10.1016/j.cell.2005.05.029
   PubMed Web of Science ®Google Scholar
• Harvey SL, Enciso G, Dephoure N, Gygi SP, Gunawardena J, Kellogg DR. A phosphatase threshold sets the level of Cdk1 activity in early mitosis in budding yeast. Mol Biol Cell 2011; 22:3595-608; PMID:21849476; http://dx.doi.org/10.1091/mbc.E11-04-0340
   PubMed Web of Science ®Google Scholar
• Tang Z, Coleman TR, Dunphy WG. Two distinct mechanisms for negative regulation of the Wee1 protein kinase. Embo J 1993; 12:3427-36; PMID:7504624
   PubMed Web of Science ®Google Scholar
• Mueller PR, Coleman TR, Dunphy WG. Cell cycle regulation of a Xenopus Wee1-like kinase. Mol Biol Cell 1995; 6:119-34; PMID:7749193; http://dx.doi.org/10.1091/mbc.6.1.119
   PubMed Web of Science ®Google Scholar
• Deibler RW, Kirschner MW. Quantitative reconstitution of mitotic CDK1 activation in somatic cell extracts. Mol Cell 2010; 37:753-67; PMID:20347419; http://dx.doi.org/10.1016/j.molcel.2010.02.023
   PubMed Web of Science ®Google Scholar
• Kim SY, Song EJ, Lee KJ, Ferrell JE Jr. Multisite M-phase phosphorylation of Xenopus Wee1A. Mol Cell Biol 2005; 25:10580-90; PMID:16287869; http://dx.doi.org/10.1128/MCB.25.23.10580-10590.2005
   PubMed Web of Science ®Google Scholar
• Watanabe N, Broome M, Hunter T. Regulation of the human Wee1Hu CDK tyrosine 15-kinase during the cell cycle. EMBO J 1995; 14:1878-91; PMID:7743995
   PubMed Web of Science ®Google Scholar
• Hoffman I, Clarke PR, Marcote MJ, Karsenti E, Draetta G. Phosphorylation and activation of human cdc25-C by cdc2-cyclin B and its involvement in the self amplification of MPF at mitosis. EMBO J 1993; 12:53-63; PMID:8428594
   PubMed Web of Science ®Google Scholar
• Izumi T, Maller JL. Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase. Mol Biol Cell 1993; 12:1337-50; http://dx.doi.org/10.1091/mbc.4.12.1337
   Google Scholar
• Pal G, Paraz MT, Kellogg DR. Regulation of Mih1/Cdc25 by protein phosphatase 2A and casein kinase 1. J Cell Biol 2008; 180:931-45; PMID:18316413; http://dx.doi.org/10.1083/jcb.200711014
   PubMed Web of Science ®Google Scholar
• Lu LX, Domingo-Sananes MR, Huzarska M, Novak B, Gould KL. Multisite phosphoregulation of Cdc25 activity refines the mitotic entrance and exit switches. Proc Natl Acad Sci U S A 2012; 109:9899-904; PMID:22665807; http://dx.doi.org/10.1073/pnas.1201366109
   PubMed Web of Science ®Google Scholar
• Kumagai A, Dunphy WG. Regulation of the cdc25 protein during the cell cycle in Xenopus extracts. Cell 1992; 70:139-51; PMID:1623517; http://dx.doi.org/10.1016/0092-8674(92)90540-S
   PubMed Web of Science ®Google Scholar
• Kovelman R, Russell P. Stockpiling of Cdc25 during a DNA replication checkpoint in Schizosaccharomyces pombe. Molec Cell Biol 1996; 16:86-93; PMID:8524332; http://dx.doi.org/10.1128/MCB.16.1.86
   PubMed Web of Science ®Google Scholar
• Trunnell NB, Poon AC, Kim SY, Ferrell JE Jr. Ultrasensitivity in the Regulation of Cdc25C by Cdk1. Mol Cell 2011; 41:263-74; PMID:21292159; http://dx.doi.org/10.1016/j.molcel.2011.01.012
   PubMed Web of Science ®Google Scholar
• Wicky S, Tjandra H, Schieltz D, Yates J 3rd, Kellogg DR. The Zds proteins control entry into mitosis and target protein phosphatase 2A to the Cdc25 phosphatase. Mol Biol Cell 2011; 22:20-32; PMID:21119008; http://dx.doi.org/10.1091/mbc.E10-06-0487
   PubMed Web of Science ®Google Scholar
• Izumi T, Maller JL. Phosphorylation and activation of the Xenopus Cdc25 phosphatase in the absence of Cdc2 and Cdk2 kinase activity. Mol Biol Cell 1995; 6:215-6; PMID:7787247; http://dx.doi.org/10.1091/mbc.6.2.215
   PubMed Web of Science ®Google Scholar
• Peng CY, Graves PR, Thoma RS, Wu Z, Shaw AS, Piwnica-Worms H. Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216. Science 1997; 277:1501-5; PMID:9278512; http://dx.doi.org/10.1126/science.277.5331.1501
   PubMed Web of Science ®Google Scholar
• Kumagai A, Yakowec PS, Dunphy WG. 14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts. Mol Biol Cell 1998; 9:345-54; PMID:9450960; http://dx.doi.org/10.1091/mbc.9.2.345
   PubMed Web of Science ®Google Scholar
• Kinoshita N, Yamano H, Niwa H, Yoshida T, Yangida M. Negative regulation of mitosis by the fission yeast protein phosphatase ppa2. Genes Dev 1993; 7:1059-71; PMID:8389306; http://dx.doi.org/10.1101/gad.7.6.1059
   PubMed Web of Science ®Google Scholar
• Chica N, Rozalen AE, Perez-Hidalgo L, Rubio A, Novak B, Moreno S. Nutritional Control of Cell Size by the Greatwall-Endosulfine-PP2A.B55 Pathway. Curr Biol 2016; 26:319-30; PMID:26776736; http://dx.doi.org/10.1016/j.cub.2015.12.035
   PubMed Web of Science ®Google Scholar
• Aligue R, Wu L, Russell P. Regulation of Schizosaccharomyces pombe Wee1 tyrosine kinase. J Biol Chem 1997; 272:13320-5; PMID:9148953; http://dx.doi.org/10.1074/jbc.272.20.13320
   PubMed Web of Science ®Google Scholar
• Creanor J, Mitchison JM. The kinetics of the B cyclin p56cdc13 and the phosphatase p80cdc25 during the cell cycle of the fission yeast Schizosaccharomyces pombe. J Cell Sci 1996; 109(Pt 6):1647-53; PMID:8799851
   PubMed Web of Science ®Google Scholar
• Raspelli E, Cassani C, Chiroli E, Fraschini R. Budding yeast Swe1 is involved in the control of mitotic spindle elongation and is regulated by Cdc14 phosphatase during mitosis. The J Biol Chem 2015; 290:6006; PMID:25750263; http://dx.doi.org/10.1074/jbc.A114.590984
   PubMed Web of Science ®Google Scholar
• Lahoz A, Alcaide-Gavilan M, Daga RR, Jimenez J. Antagonistic roles of PP2A-Pab1 and Etd1 in the control of cytokinesis in fission yeast. Genetics 2010; 186:1261-70; PMID:20876564; http://dx.doi.org/10.1534/genetics.110.121368
   PubMed Web of Science ®Google Scholar
• Trautmann S, Wolfe BA, Jorgensen P, Tyers M, Gould KL, McCollum D. Fission yeast Clp1p phosphatase regulates G2/M transition and coordination of cytokinesis with cell cycle progression. Curr Biol 2001; 11:931-40; PMID:11448769; http://dx.doi.org/10.1016/S0960-9822(01)00268-8
   PubMed Web of Science ®Google Scholar
• Wolfe BA, Gould KL. Fission yeast Clp1p phosphatase affects G2/M transition and mitotic exit through Cdc25p inactivation. Embo J 2004; 23:919-29; PMID:14765109; http://dx.doi.org/10.1038/sj.emboj.7600103
   PubMed Web of Science ®Google Scholar
• Esteban V, Blanco M, Cueille N, Simanis V, Moreno S, Bueno A. A role for the Cdc14-family phosphatase Flp1p at the end of the cell cycle in controlling the rapid degradation of the mitotic inducer Cdc25p in fission yeast. J Cell Sci 2004; 117:2461-8; PMID:15128870; http://dx.doi.org/10.1242/jcs.01107
   PubMed Web of Science ®Google Scholar
• Shulewitz MJ, Inouye CJ, Thorner J. Hsl7 localizes to a septin ring and serves as an adapter in regulatory pathway that relieves tyrosine phosphorylation of Cdc28 protein kinase in Saccharomyces cerevisiae. Mol Cell Biol 1999; 19:7123-37; PMID:10490648; http://dx.doi.org/10.1128/MCB.19.10.7123
   PubMed Web of Science ®Google Scholar
• Sreenivasan A, Kellogg D. The Elm1 kinase functions in a mitotic signaling network in budding yeast. Mol Cell Biol 1999; 19:7983-94; PMID:10567524; http://dx.doi.org/10.1128/MCB.19.12.7983
   PubMed Web of Science ®Google Scholar
• Sia RAL, Bardes ESG, Lew DJ. Control of Swe1p degradation by the morphogenesis checkpoint. EMBO J 1998; 17:6678-88; PMID:9822611; http://dx.doi.org/10.1093/emboj/17.22.6678
   PubMed Web of Science ®Google Scholar
• Nurse P, Thuriaux P. Regulatory genes controlling mitosis in the fission yeast Schizosaccharomyces pombe. Genetics 1980; 96:627-37; PMID:7262540
   PubMed Web of Science ®Google Scholar
• Moreno S, Hayles J, Nurse P. Regulation of p34cdc2 protein kinase during mitosis. Cell 1989; 58:361-72; PMID:2665944; http://dx.doi.org/10.1016/0092-8674(89)90850-7
   PubMed Web of Science ®Google Scholar
• Lianga N, Williams EC, Kennedy EK, Dore C, Pilon S, Girard SL, Deneault JS, Rudner AD. A Wee1 checkpoint inhibits anaphase onset. J Cell Biol 2013; 201:843-62; PMID:23751495; http://dx.doi.org/10.1083/jcb.201212038
   PubMed Web of Science ®Google Scholar
• Toledo CM, Ding Y, Hoellerbauer P, Davis RJ, Basom R, Girard EJ, Lee E, Corrin P, Hart T, Bolouri H, et al. Genome-wide CRISPR-Cas9 screens reveal loss of redundancy between PKMYT1 and WEE1 in glioblastoma stem-like cells. Cell Rep 2015; 13:2425-39; PMID:26673326; http://dx.doi.org/10.1016/j.celrep.2015.11.021
   PubMed Web of Science ®Google Scholar
• Stumpff J, Kellogg DR, Krohne KA, Su TT. Drosophila Wee1 interacts with members of the gammaTURC and is required for proper mitotic-spindle morphogenesis and positioning. Curr Biol 2005; 15:1525-34; PMID:16139207; http://dx.doi.org/10.1016/j.cub.2005.07.031
   PubMed Web of Science ®Google Scholar
• Lucena R, Dephoure N, Gygi SP, Kellogg DR, Tallada VA, Daga RR, Jimenez J. Nucleocytoplasmic transport in the midzone membrane domain controls yeast mitotic spindle disassembly. J Cell Biol 2015; 209:387-402; PMID:25963819; http://dx.doi.org/10.1083/jcb.201412144
   PubMed Web of Science ®Google Scholar
• Anderson CW, Baum PR, Gesteland RF. Processing of adenovirus 2-induced proteins. J Virol 1973; 12:241-52; PMID:4747985
   PubMed Web of Science ®Google Scholar
• Moreno S, Klar A, Nurse P. Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol 1991; 194:795-823
   PubMed Web of Science ®Google Scholar