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Volumn 79, Issue 5, 2008, Pages 991-998

CDC25B acts as a potential target of PRKACA in fertilized mouse eggs

Author keywords

CDC25B; M phase promoting factor; Mouse fertilized eggs; PRKACA

Indexed keywords

ANTIBODY; BUCLADESINE; CYCLIC AMP DEPENDENT PROTEIN KINASE; MATURATION PROMOTING FACTOR; MESSENGER RNA; PROTEIN TYROSINE PHOSPHATASE;

EID: 55549110382     PISSN: 00063363     EISSN: 15297268     Source Type: Journal    
DOI: 10.1095/biolreprod.108.068205     Document Type: Article
Times cited : (18)

References (53)
  • 1
    • 0031297716 scopus 로고    scopus 로고
    • Myt1: A Wee1-type kinase that phosphorylates Cdc2 on residue Thr14
    • Fattaey A, Booher RN. Myt1: a Wee1-type kinase that phosphorylates Cdc2 on residue Thr14. Prog Cell Cycle Res 1997; 3:233-240.
    • (1997) Prog Cell Cycle Res , vol.3 , pp. 233-240
    • Fattaey, A.1    Booher, R.N.2
  • 2
    • 0027510249 scopus 로고
    • Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15
    • McGowan CH, Russell P. Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15. EMBO J 1993; 12:75-85.
    • (1993) EMBO J , vol.12 , pp. 75-85
    • McGowan, C.H.1    Russell, P.2
  • 3
    • 0028783413 scopus 로고
    • Myt1: A membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15
    • Mueller PR, Coleman TR, Kumagai A, Dunphy WG. Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15. Science 1995; 270:86-90.
    • (1995) Science , vol.270 , pp. 86-90
    • Mueller, P.R.1    Coleman, T.R.2    Kumagai, A.3    Dunphy, W.G.4
  • 4
    • 0026616796 scopus 로고
    • Inactivation of the p34cdc2-cyclin B complex by the human WEE1 tyrosine kinase
    • Parker LL, Piwnica-Worms H. Inactivation of the p34cdc2-cyclin B complex by the human WEE1 tyrosine kinase. Science 1992; 257:1955-1957.
    • (1992) Science , vol.257 , pp. 1955-1957
    • Parker, L.L.1    Piwnica-Worms, H.2
  • 5
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan DO. Principles of CDK regulation. Nature 1995; 374:131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 7
    • 0043066731 scopus 로고    scopus 로고
    • Regulating mammalian checkpoints through Cdc25 inactivation
    • Donzelli M, Draetta GF. Regulating mammalian checkpoints through Cdc25 inactivation. EMBO Rep 2003; 4:671-677.
    • (2003) EMBO Rep , vol.4 , pp. 671-677
    • Donzelli, M.1    Draetta, G.F.2
  • 8
    • 33750618926 scopus 로고    scopus 로고
    • Mitotic phosphatases: No longer silent partners
    • Trinkle-Mulcahy L, Lamond AI. Mitotic phosphatases: no longer silent partners. Curr Opin Cell Biol 2006; 18:623-631.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 623-631
    • Trinkle-Mulcahy, L.1    Lamond, A.I.2
  • 9
    • 0028022034 scopus 로고
    • Activation of the phosphatase activity of human cdc25A by a cdk2-cyclin E dependent phosphorylation at the G1/S transition
    • Hoffmann I, Draetta G, Karsenti E. Activation of the phosphatase activity of human cdc25A by a cdk2-cyclin E dependent phosphorylation at the G1/S transition. EMBO J 1994; 13:4302-4310.
    • (1994) EMBO J , vol.13 , pp. 4302-4310
    • Hoffmann, I.1    Draetta, G.2    Karsenti, E.3
  • 10
    • 0033629383 scopus 로고    scopus 로고
    • Cell cycle regulation by the Cdc25 phosphatase family
    • Nilsson I, Hoffmann I. Cell cycle regulation by the Cdc25 phosphatase family. Prog Cell Cycle Res 2000; 4:107-114.
    • (2000) Prog Cell Cycle Res , vol.4 , pp. 107-114
    • Nilsson, I.1    Hoffmann, I.2
  • 11
    • 0028168379 scopus 로고
    • Activation of p34cdc2 protein kinase by microinjection of human CDC25C into mammalian cells. Requirement for prior phosphorylation of CDC25C by p34cdc2 on sites phosphorylated at mitosis
    • Strausfeld U, Fernandez A, Capony JP, Girard F, Lautredou N, Derancourt J, Labbe JC, Lamb NJ. Activation of p34cdc2 protein kinase by microinjection of human CDC25C into mammalian cells. Requirement for prior phosphorylation of CDC25C by p34cdc2 on sites phosphorylated at mitosis. J Biol Chem 1994; 269:5989-6000.
    • (1994) J Biol Chem , vol.269 , pp. 5989-6000
    • Strausfeld, U.1    Fernandez, A.2    Capony, J.P.3    Girard, F.4    Lautredou, N.5    Derancourt, J.6    Labbe, J.C.7    Lamb, N.J.8
  • 13
    • 0033538847 scopus 로고    scopus 로고
    • Cdc25B and Cdc25C differ markedly in their properties as initiators of mitosis
    • Karlsson C, Katich S, Hagting A, Hoffmann I, Pines J. Cdc25B and Cdc25C differ markedly in their properties as initiators of mitosis. J Cell Biol 1999; 146:573-584.
    • (1999) J Cell Biol , vol.146 , pp. 573-584
    • Karlsson, C.1    Katich, S.2    Hagting, A.3    Hoffmann, I.4    Pines, J.5
  • 14
    • 33750983644 scopus 로고    scopus 로고
    • Knockdown of the cAMP-dependent protein kinase (PKA) Type Ialpha regulatory subunit in mouse oocytes disrupts meiotic arrest and results in meiotic spindle defects
    • Duncan FE, Moss SB, Williams CJ. Knockdown of the cAMP-dependent protein kinase (PKA) Type Ialpha regulatory subunit in mouse oocytes disrupts meiotic arrest and results in meiotic spindle defects. Dev Dyn 2006; 235:2961-2968.
    • (2006) Dev Dyn , vol.235 , pp. 2961-2968
    • Duncan, F.E.1    Moss, S.B.2    Williams, C.J.3
  • 15
    • 33746394321 scopus 로고    scopus 로고
    • An active protein kinase A (PKA) is involved in meiotic arrest of rat growing oocytes
    • Kovo M, Kandli-Cohen M, Ben-Haim M, Galiani D, Carr DW, Dekel N. An active protein kinase A (PKA) is involved in meiotic arrest of rat growing oocytes. Reproduction 2006; 132:33-43.
    • (2006) Reproduction , vol.132 , pp. 33-43
    • Kovo, M.1    Kandli-Cohen, M.2    Ben-Haim, M.3    Galiani, D.4    Carr, D.W.5    Dekel, N.6
  • 16
    • 0022595332 scopus 로고
    • Involvement of cAMP-dependent protein kinase and protein phosphorylation in regulation of mouse oocyte maturation
    • Bornslaeger EA, Mattei P, Schultz RM. Involvement of cAMP-dependent protein kinase and protein phosphorylation in regulation of mouse oocyte maturation. Dev Biol 1986; 114:453-462.
    • (1986) Dev Biol , vol.114 , pp. 453-462
    • Bornslaeger, E.A.1    Mattei, P.2    Schultz, R.M.3
  • 17
    • 0027458578 scopus 로고
    • Inhibition of mos-induced oocyte maturation by protein kinase A
    • Daar I, Yew N, Vande Woude GF. Inhibition of mos-induced oocyte maturation by protein kinase A. J Cell Biol 1993; 120:1197-1202.
    • (1993) J Cell Biol , vol.120 , pp. 1197-1202
    • Daar, I.1    Yew, N.2    Vande Woude, G.F.3
  • 18
    • 0032504966 scopus 로고    scopus 로고
    • Inactivation of protein kinase A is not required for c-mos translation during meiotic maturation of Xenopus oocytes
    • Faure S, Morin N, Dorée M. Inactivation of protein kinase A is not required for c-mos translation during meiotic maturation of Xenopus oocytes. Oncogene 1998; 17:1215-1221.
    • (1998) Oncogene , vol.17 , pp. 1215-1221
    • Faure, S.1    Morin, N.2    Dorée, M.3
  • 19
    • 0028228544 scopus 로고
    • Protein kinase A acts at multiple points to inhibit Xenopus oocyte maturation
    • Matten W, Daar I, Vande Woude GF. Protein kinase A acts at multiple points to inhibit Xenopus oocyte maturation. Mol Cell Biol 1994; 14:4419-4426.
    • (1994) Mol Cell Biol , vol.14 , pp. 4419-4426
    • Matten, W.1    Daar, I.2    Vande Woude, G.F.3
  • 20
    • 0028138344 scopus 로고
    • A role for cAMP-dependent protein kinase in early embryonic divisions
    • Grieco D, Avvedimento EV, Gottesman ME. A role for cAMP-dependent protein kinase in early embryonic divisions. Proc Natl Acad Sci U S A 1994; 91:9896-9900.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9896-9900
    • Grieco, D.1    Avvedimento, E.V.2    Gottesman, M.E.3
  • 21
    • 0024550140 scopus 로고
    • Starfish oocyte maturation: Evidence for a cyclic AMP-dependent inhibitory pathway
    • Meijer L, Dostmann W, Genieser HG, Butt E, Jastorff B. Starfish oocyte maturation: evidence for a cyclic AMP-dependent inhibitory pathway. Dev Biol 1989; 133:58-66.
    • (1989) Dev Biol , vol.133 , pp. 58-66
    • Meijer, L.1    Dostmann, W.2    Genieser, H.G.3    Butt, E.4    Jastorff, B.5
  • 22
    • 21644475592 scopus 로고    scopus 로고
    • Regulation of the G(2)/M transition in Xenopus oocytes by the cAMPdependent protein kinase
    • Eyers PA, Liu J, Hayashi NR, Lewellyn AL, Gautier J, Maller JL. Regulation of the G(2)/M transition in Xenopus oocytes by the cAMPdependent protein kinase. J Biol Chem 2005; 280:24339-24346.
    • (2005) J Biol Chem , vol.280 , pp. 24339-24346
    • Eyers, P.A.1    Liu, J.2    Hayashi, N.R.3    Lewellyn, A.L.4    Gautier, J.5    Maller, J.L.6
  • 23
    • 24944486339 scopus 로고    scopus 로고
    • Wee1B is an oocyte-specific kinase involved in the control of meiotic arrest in the mouse
    • Han SJ, Chen R, Paronetto MP, Conti M. Wee1B is an oocyte-specific kinase involved in the control of meiotic arrest in the mouse. Curr Biol 2005; 15:1670-1676.
    • (2005) Curr Biol , vol.15 , pp. 1670-1676
    • Han, S.J.1    Chen, R.2    Paronetto, M.P.3    Conti, M.4
  • 24
    • 0037168424 scopus 로고    scopus 로고
    • G2 arrest in Xenopus oocytes depends on phosphorylation of cdc25 by protein kinase A
    • Duckworth BC, Weaver JS, Ruderman JV. G2 arrest in Xenopus oocytes depends on phosphorylation of cdc25 by protein kinase A. Proc Natl Acad Sci U S A 2002; 99:16794-16799.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16794-16799
    • Duckworth, B.C.1    Weaver, J.S.2    Ruderman, J.V.3
  • 26
    • 35848940699 scopus 로고    scopus 로고
    • Polo-like kinase 1 may regulate G2/M transition of mouse fertilized eggs by means of inhibiting the phosphorylation of Tyr 15 of Cdc2
    • Zhang Z, Su WH, Feng C, Yu DH, Cui C, Xu XY, Yu BZ. Polo-like kinase 1 may regulate G2/M transition of mouse fertilized eggs by means of inhibiting the phosphorylation of Tyr 15 of Cdc2. Mol Reprod Dev 2007; 74:1247-1254.
    • (2007) Mol Reprod Dev , vol.74 , pp. 1247-1254
    • Zhang, Z.1    Su, W.H.2    Feng, C.3    Yu, D.H.4    Cui, C.5    Xu, X.Y.6    Yu, B.Z.7
  • 27
    • 0030889816 scopus 로고    scopus 로고
    • Activation of protein kinase C after fertilization is required for remodeling the mouse egg into the zygote
    • Gallicano GI, McGaughey RW, Capco DG. Activation of protein kinase C after fertilization is required for remodeling the mouse egg into the zygote. Mol Reprod Dev 1997; 46:587-601.
    • (1997) Mol Reprod Dev , vol.46 , pp. 587-601
    • Gallicano, G.I.1    McGaughey, R.W.2    Capco, D.G.3
  • 28
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer JC, Cantley LC, Yaffe MB. Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res 2003; 31:3635-3641.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 29
    • 0020771377 scopus 로고
    • Regulation of mouse oocyte meiotic maturation: Implication of a decrease in oocyte cAMP and protein dephosphorylation in commitment to resume meiosis
    • Schultz RM, Montgomery RR, Belanoff JR. Regulation of mouse oocyte meiotic maturation: implication of a decrease in oocyte cAMP and protein dephosphorylation in commitment to resume meiosis. Dev Biol 1983; 97:264-273.
    • (1983) Dev Biol , vol.97 , pp. 264-273
    • Schultz, R.M.1    Montgomery, R.R.2    Belanoff, J.R.3
  • 33
    • 11244350166 scopus 로고    scopus 로고
    • Protein kinase A regulates cell cycle progression of mouse fertilized eggs by means of MPF
    • Yu B, Wang Y, Liu Y, Liu Y, Li X, Wu D, Zong Z, Zhang J, Yu D. Protein kinase A regulates cell cycle progression of mouse fertilized eggs by means of MPF. Dev Dyn 2005; 232:98-105.
    • (2005) Dev Dyn , vol.232 , pp. 98-105
    • Yu, B.1    Wang, Y.2    Liu, Y.3    Liu, Y.4    Li, X.5    Wu, D.6    Zong, Z.7    Zhang, J.8    Yu, D.9
  • 34
    • 0037154998 scopus 로고    scopus 로고
    • Translational and post-translational modifications in meiosis of the mammalian oocyte
    • Josefsberg LB, Dekel N. Translational and post-translational modifications in meiosis of the mammalian oocyte. Mol Cell Endocrinol 2002; 187:161-171.
    • (2002) Mol Cell Endocrinol , vol.187 , pp. 161-171
    • Josefsberg, L.B.1    Dekel, N.2
  • 35
    • 33748804188 scopus 로고    scopus 로고
    • Increase in intracellular cAMP is a prerequisite signal for initiation of physiological oocyte meiotic maturation in the hydrozoan Cytaeis uchidae
    • Takeda N, Kyozuka K, Deguchi R. Increase in intracellular cAMP is a prerequisite signal for initiation of physiological oocyte meiotic maturation in the hydrozoan Cytaeis uchidae. Dev Biol 2006; 298:248-258.
    • (2006) Dev Biol , vol.298 , pp. 248-258
    • Takeda, N.1    Kyozuka, K.2    Deguchi, R.3
  • 36
    • 0030884275 scopus 로고    scopus 로고
    • A dual-specificity phosphatase Cdc25B is an unstable protein and triggers p34 (cdc2)/cyclin B activation in hamster BHK21 cells arrested with hydroxyurea
    • Nishijima H, Nishitani H, Seki T, Nishimoto T. A dual-specificity phosphatase Cdc25B is an unstable protein and triggers p34 (cdc2)/cyclin B activation in hamster BHK21 cells arrested with hydroxyurea. J Cell Biol 1997; 138:1105-1116.
    • (1997) J Cell Biol , vol.138 , pp. 1105-1116
    • Nishijima, H.1    Nishitani, H.2    Seki, T.3    Nishimoto, T.4
  • 37
    • 0024978338 scopus 로고
    • Cyclin synthesis drives the early embryonic cell cycle
    • Murray AW, Kirschner MW. Cyclin synthesis drives the early embryonic cell cycle. Nature 1989; 339:275-280.
    • (1989) Nature , vol.339 , pp. 275-280
    • Murray, A.W.1    Kirschner, M.W.2
  • 38
    • 0024978344 scopus 로고
    • The role of cyclin synthesis and degradation in the control of maturation promoting factor activity
    • Murray AW, Solomon MJ, Kirschner MW. The role of cyclin synthesis and degradation in the control of maturation promoting factor activity. Nature 1989; 339:280-286.
    • (1989) Nature , vol.339 , pp. 280-286
    • Murray, A.W.1    Solomon, M.J.2    Kirschner, M.W.3
  • 39
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin AJ, Tanner JW, Allen PM, Shaw AS. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996; 84:889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 42
    • 0030611095 scopus 로고    scopus 로고
    • Mitotic and G2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216
    • 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; 277:1501-1505.
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.Y.1    Graves, P.R.2    Thoma, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 43
    • 0030867582 scopus 로고    scopus 로고
    • Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regulation through Cdc25
    • Sanchez Y, Wong C, Thoma RS, Richman R, Wu Z, Piwnica-Worms H, Elledge SJ. Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25. Science 1997; 277:1497-1501.
    • (1997) Science , vol.277 , pp. 1497-1501
    • Sanchez, Y.1    Wong, C.2    Thoma, R.S.3    Richman, R.4    Wu, Z.5    Piwnica-Worms, H.6    Elledge, S.J.7
  • 44
    • 0035913162 scopus 로고    scopus 로고
    • Cdc25B activity is regulated by 14-3-3
    • Forrest A, Gabrielli B. Cdc25B activity is regulated by 14-3-3. Oncogene 2001; 20:4393-4401.
    • (2001) Oncogene , vol.20 , pp. 4393-4401
    • Forrest, A.1    Gabrielli, B.2
  • 45
    • 0041707637 scopus 로고    scopus 로고
    • 14-3-3 acts as an intramolecular bridge to regulate cdc25B localization and activity
    • Giles N, Forrest A, Gabrielli B. 14-3-3 acts as an intramolecular bridge to regulate cdc25B localization and activity. J Biol Chem 2003; 278:28580-28587.
    • (2003) J Biol Chem , vol.278 , pp. 28580-28587
    • Giles, N.1    Forrest, A.2    Gabrielli, B.3
  • 46
    • 0031906844 scopus 로고    scopus 로고
    • 14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts
    • 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; 9:345-354.
    • (1998) Mol Biol Cell , vol.9 , pp. 345-354
    • Kumagai, A.1    Yakowec, P.S.2    Dunphy, W.G.3
  • 47
    • 0034713226 scopus 로고    scopus 로고
    • Centrosomal and cytoplasmic Cdc2/cyclin B1 activation precedes nuclear mitotic events
    • De Souza CP, Ellem KA, Gabrielli BG. Centrosomal and cytoplasmic Cdc2/cyclin B1 activation precedes nuclear mitotic events. Exp Cell Res 2000; 257:11-21.
    • (2000) Exp Cell Res , vol.257 , pp. 11-21
    • De Souza, C.P.1    Ellem, K.A.2    Gabrielli, B.G.3
  • 48
    • 0037322744 scopus 로고    scopus 로고
    • Active cyclin B1-Cdk1 first appears on centrosomes in prophase
    • Jackman M, Lindon C, Nigg EA, Pines J. Active cyclin B1-Cdk1 first appears on centrosomes in prophase. Nat Cell Biol 2003; 5:143-148.
    • (2003) Nat Cell Biol , vol.5 , pp. 143-148
    • Jackman, M.1    Lindon, C.2    Nigg, E.A.3    Pines, J.4
  • 49
    • 0029937532 scopus 로고    scopus 로고
    • Cytoplasmic accumulation of cdc25B phosphatase in mitosis triggers centrosomal microtubule nucleation in HeLa cells
    • Gabrielli BG, De Souza CP, Tonks ID, Clark JM, Hayward NK, Ellem KA. Cytoplasmic accumulation of cdc25B phosphatase in mitosis triggers centrosomal microtubule nucleation in HeLa cells. J Cell Sci 1996; 109:1081-1093.
    • (1996) J Cell Sci , vol.109 , pp. 1081-1093
    • Gabrielli, B.G.1    De Souza, C.P.2    Tonks, I.D.3    Clark, J.M.4    Hayward, N.K.5    Ellem, K.A.6
  • 50
    • 26444493574 scopus 로고    scopus 로고
    • Cdc25B cooperates with Cdc25A to induce mitosis but has a unique role in activating cyclin B1-Cdk1 at the centrosome
    • Lindqvist A, Källström H, Lundgren A, Barsoum E, Rosenthal CK. Cdc25B cooperates with Cdc25A to induce mitosis but has a unique role in activating cyclin B1-Cdk1 at the centrosome. J Cell Biol 2005; 171:35-45.
    • (2005) J Cell Biol , vol.171 , pp. 35-45
    • Lindqvist, A.1    Källström, H.2    Lundgren, A.3    Barsoum, E.4    Rosenthal, C.K.5
  • 51
    • 8744229083 scopus 로고    scopus 로고
    • Characterisation of Cdc25B localisation and nuclear export during the cell cycle and in response to stress
    • Lindqvist A, Källström H, Karlsson Rosenthal C. Characterisation of Cdc25B localisation and nuclear export during the cell cycle and in response to stress. J Cell Sci 2004; 117:4979-4990.
    • (2004) J Cell Sci , vol.117 , pp. 4979-4990
    • Lindqvist, A.1    Källström, H.2    Karlsson Rosenthal, C.3
  • 53
    • 4644262376 scopus 로고    scopus 로고
    • When the checkpoints have gone: Insights into Cdc25 functional activation
    • Margolis SS, Kornbluth S. When the checkpoints have gone: insights into Cdc25 functional activation. Cell Cycle 2004; 3:425-428.
    • (2004) Cell Cycle , vol.3 , pp. 425-428
    • Margolis, S.S.1    Kornbluth, S.2


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