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Volumn 8, Issue 1, 2013, Pages

The Role of 14-3-3ε Interaction with Phosphorylated Cdc25B at Its Ser321 in the Release of the Mouse Oocyte from Prophase I Arrest

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CDC25B PROTEIN; ISOPROTEIN; PROTEIN 14 3 3; PROTEIN 14 3 3 EPSILON; PROTEIN TYROSINE PHOSPHATASE; SERINE; UNCLASSIFIED DRUG;

EID: 84872255347     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0053633     Document Type: Article
Times cited : (29)

References (46)
  • 1
    • 32244436114 scopus 로고    scopus 로고
    • New pathways from PKA to the Cdc2/cyclin B complex in oocytes: Wee1B as a potential PKA substrate
    • Han SJ, Conti M, (2006) New pathways from PKA to the Cdc2/cyclin B complex in oocytes: Wee1B as a potential PKA substrate. Cell Cycle 5: 227-231.
    • (2006) Cell Cycle , vol.5 , pp. 227-231
    • Han, S.J.1    Conti, M.2
  • 2
    • 24944486339 scopus 로고    scopus 로고
    • Wee1B is an oocytes-specific kinase involved in the control of meiotic arrest in the mouse
    • Han SJ, Chen R, Paronrtto MP, Conti M, (2005) Wee1B is an oocytes-specific kinase involved in the control of meiotic arrest in the mouse. Curr Biol 15: 1670-1676.
    • (2005) Curr Biol , vol.15 , pp. 1670-1676
    • Han, S.J.1    Chen, R.2    Paronrtto, M.P.3    Conti, M.4
  • 3
    • 33947646873 scopus 로고    scopus 로고
    • Cdc25 phosphatases: structure, specificity and mechanism
    • Rudolph J, (2007) Cdc25 phosphatases: structure, specificity and mechanism. Biochemistry 46: 3595-3604.
    • (2007) Biochemistry , vol.46 , pp. 3595-3604
    • Rudolph, J.1
  • 4
    • 34250865564 scopus 로고    scopus 로고
    • Cdc25 phosphatases in cancer cells: key player? Good target
    • Boutros R, Lobjois V, Ducommun B, (2007) Cdc25 phosphatases in cancer cells: key player? Good target? Nat Rev Cancer 7: 495-507.
    • (2007) Nat Rev Cancer , vol.7 , pp. 495-507
    • Boutros, R.1    Lobjois, V.2    Ducommun, B.3
  • 5
    • 0036544855 scopus 로고    scopus 로고
    • Cdc25B phosphatases is required for resumption of meiosis during oocyte maturation
    • Lincoln AJ, Wickramasinghe D, Stein P, Schultz RM, Palko ME, et al. (2002) Cdc25B phosphatases is required for resumption of meiosis during oocyte maturation. Nat Genet 30: 446-449.
    • (2002) Nat Genet , vol.30 , pp. 446-449
    • Lincoln, A.J.1    Wickramasinghe, D.2    Stein, P.3    Schultz, R.M.4    Palko, M.E.5
  • 7
    • 61449152905 scopus 로고    scopus 로고
    • PKA and Cdc25B: at last connected
    • Schultz R, (2009) PKA and Cdc25B: at last connected. Cell Cycle 8: 516-517.
    • (2009) Cell Cycle , vol.8 , pp. 516-517
    • Schultz, R.1
  • 8
    • 76149133667 scopus 로고    scopus 로고
    • Wee1B, Myt1, and Cdc25 function in distinct compartments of the mouse oocyte to control meiotic resumption
    • Oh JS, Han SJ, Conti M, (2010) Wee1B, Myt1, and Cdc25 function in distinct compartments of the mouse oocyte to control meiotic resumption. J Cell Biol 188: 199-207.
    • (2010) J Cell Biol , vol.188 , pp. 199-207
    • Oh, J.S.1    Han, S.J.2    Conti, M.3
  • 9
    • 57149118858 scopus 로고    scopus 로고
    • Protein kinase A modulates Cdc25B activity during meiotic resumption of mouse oocytes
    • Zhang Y, Zhang Z, Xu XY, Li XS, Yu M, et al. (2008) Protein kinase A modulates Cdc25B activity during meiotic resumption of mouse oocytes. Dev Dyn 237: 3777-3786.
    • (2008) Dev Dyn , vol.237 , pp. 3777-3786
    • Zhang, Y.1    Zhang, Z.2    Xu, X.Y.3    Li, X.S.4    Yu, M.5
  • 10
    • 42649135556 scopus 로고    scopus 로고
    • Cdc25A phosphatase controls meiosis I progression in mouse oocytes
    • Solc P, Saskova A, Baran V, Kubelka M, Schultz RM, et al. (2008) Cdc25A phosphatase controls meiosis I progression in mouse oocytes. Dev Biol 317: 360-369.
    • (2008) Dev Biol , vol.317 , pp. 360-369
    • Solc, P.1    Saskova, A.2    Baran, V.3    Kubelka, M.4    Schultz, R.M.5
  • 12
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh C, (2004) Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. J Biochem 381: 329-342.
    • (2004) J Biochem , vol.381 , pp. 329-342
    • Mackintosh, C.1
  • 13
    • 3543035767 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins
    • Meek SEM, Lane WS, Piwnica-Worms H, (2004) Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins. J Biol Chem 279: 32046-32054.
    • (2004) J Biol Chem , vol.279 , pp. 32046-32054
    • Meek, S.E.M.1    Lane, W.S.2    Piwnica-Worms, H.3
  • 14
    • 0041312686 scopus 로고    scopus 로고
    • 14-3-3s regulate fructose-2,6- bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase
    • Rubio MP, Peggie M, Wong BHC, Morrice N, MacKintosh C, (2003) 14-3-3s regulate fructose-2,6- bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase. EMBO J 22: 3514-3523.
    • (2003) EMBO J , vol.22 , pp. 3514-3523
    • Rubio, M.P.1    Peggie, M.2    Wong, B.H.C.3    Morrice, N.4    MacKintosh, C.5
  • 15
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty MK, Morrison DK, (2004) Unlocking the code of 14-3-3. J Cell Sci 117: 1875-1884.
    • (2004) J Cell Sci , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 16
    • 33644877400 scopus 로고    scopus 로고
    • 14-3-3 proteins: a number of functions for a numbered protein
    • Bridges D, Moorhead GB, (2005) 14-3-3 proteins: a number of functions for a numbered protein. Sci STKE re10.
    • (2005) Sci STKE re10
    • Bridges, D.1    Moorhead, G.B.2
  • 17
    • 33745654966 scopus 로고    scopus 로고
    • Amino acids C-terminal to the 14-3-3 binding motif in Cdc25B affect the efficiency of 14-3-3 binding
    • Uchida S, Kubo A, Kizu R, Nakagama H, Matsunaga T, et al. (2006) Amino acids C-terminal to the 14-3-3 binding motif in Cdc25B affect the efficiency of 14-3-3 binding. J Biochem 139: 761-769.
    • (2006) J Biochem , vol.139 , pp. 761-769
    • Uchida, S.1    Kubo, A.2    Kizu, R.3    Nakagama, H.4    Matsunaga, T.5
  • 18
    • 0242389822 scopus 로고    scopus 로고
    • PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation
    • Margolis SS, Walsh S, Weiser DC, Yoshida M, Shenolikar S, et al. (2003) PP1 control of M phase entry exerted through 14-3-3-regulated Cdc25 dephosphorylation. EMBO J 22: 5734-5745.
    • (2003) EMBO J , vol.22 , pp. 5734-5745
    • Margolis, S.S.1    Walsh, S.2    Weiser, D.C.3    Yoshida, M.4    Shenolikar, S.5
  • 19
    • 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, (2002) G2 arrest in Xenopus oocytes depends on phosphorylation of Cdc25 by protein kinase A. Proc Natl Acad Sci USA 99: 16794-16799.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16794-16799
    • Duckworth, B.C.1    Weaver, J.S.2    Ruderman, J.V.3
  • 20
    • 0033561439 scopus 로고    scopus 로고
    • Maintenance of G2 arrest in the Xenopus oocyte: a role for 14-3-3-mediated inhibition of Cdc25 nuclear import
    • Yang J, Winkler K, Yoshida M, Kornbluth S, (1999) Maintenance of G2 arrest in the Xenopus oocyte: a role for 14-3-3-mediated inhibition of Cdc25 nuclear import. EMBO J 18: 2174-2183.
    • (1999) EMBO J , vol.18 , pp. 2174-2183
    • Yang, J.1    Winkler, K.2    Yoshida, M.3    Kornbluth, S.4
  • 21
    • 79953181966 scopus 로고    scopus 로고
    • Ser149 is another potential PKA phosphorylation target of Cdc25B in G2/M transition of fertilized mouse eggs
    • Xiao JY, Liu C, Hou JJ, Cheng C, Wu DD, et al. (2011) Ser149 is another potential PKA phosphorylation target of Cdc25B in G2/M transition of fertilized mouse eggs. J Biol Chem 286: 10356-10366.
    • (2011) J Biol Chem , vol.286 , pp. 10356-10366
    • Xiao, J.Y.1    Liu, C.2    Hou, J.J.3    Cheng, C.4    Wu, D.D.5
  • 22
    • 0022595332 scopus 로고
    • Involvement of cAMP-dependent protein kinase and protein phosphorylation in regulation of mouse oocyte maturation
    • Bornslaeger EA, Mattei P, Schultz RM, (1986) Involvement of cAMP-dependent protein kinase and protein phosphorylation in regulation of mouse oocyte maturation. Dev Biol 114: 453-462.
    • (1986) Dev Biol , vol.114 , pp. 453-462
    • Bornslaeger, E.A.1    Mattei, P.2    Schultz, R.M.3
  • 23
    • 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, (2006) 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 235: 2961-2968.
    • (2006) Dev Dyn , vol.235 , pp. 2961-2968
    • Duncan, F.E.1    Moss, S.B.2    Williams, C.J.3
  • 24
    • 0029905263 scopus 로고    scopus 로고
    • Roles of protein kinase A and C in spontaneous maturation and in forskolin or 3-isobutyl-1-methylxanthine maintained meiotic arrest of bovine oocytes
    • Rose-Hellekant TA, Bavister BD, (1996) Roles of protein kinase A and C in spontaneous maturation and in forskolin or 3-isobutyl-1-methylxanthine maintained meiotic arrest of bovine oocytes. Mol Reprod Dev 44: 241-249.
    • (1996) Mol Reprod Dev , vol.44 , pp. 241-249
    • Rose-Hellekant, T.A.1    Bavister, B.D.2
  • 27
    • 61449089508 scopus 로고    scopus 로고
    • Protein kinase A regulates resumption of meiosis by phosphorylation of Cdc25B in mammalian oocytes
    • Pirino G, Wescott MP, Donovan PJ, (2009) Protein kinase A regulates resumption of meiosis by phosphorylation of Cdc25B in mammalian oocytes. Cell Cycle 8: 665-670.
    • (2009) Cell Cycle , vol.8 , pp. 665-670
    • Pirino, G.1    Wescott, M.P.2    Donovan, P.J.3
  • 28
    • 55549110382 scopus 로고    scopus 로고
    • Cdc25B Acts as a Potential Target of PRKACA in Fertilized Mouse Eggs
    • Cui C, Zhao HM, Zhang Z, Zong ZH, Feng C, et al. (2008) Cdc25B Acts as a Potential Target of PRKACA in Fertilized Mouse Eggs. Biol Reprod 79: 991-998.
    • (2008) Biol Reprod , vol.79 , pp. 991-998
    • Cui, C.1    Zhao, H.M.2    Zhang, Z.3    Zong, Z.H.4    Feng, C.5
  • 29
    • 11244350166 scopus 로고    scopus 로고
    • Protein kinase A regulates cell cycle progression of mouse fertilized eggs by means of MPF
    • Yu BZ, Wang YJ, Liu Y, Liu Y, Li XS, et al. (2005) Protein kinase A regulates cell cycle progression of mouse fertilized eggs by means of MPF. Dev Dyn 232: 98-105.
    • (2005) Dev Dyn , vol.232 , pp. 98-105
    • Yu, B.Z.1    Wang, Y.J.2    Liu, Y.3    Liu, Y.4    Li, X.S.5
  • 30
    • 33744544172 scopus 로고    scopus 로고
    • 14-3-3 proteins in cell cycle regulation
    • Hermeking H, Benzinger A, (2006) 14-3-3 proteins in cell cycle regulation. Semin Cancer Biol 16: 183-192.
    • (2006) Semin Cancer Biol , vol.16 , pp. 183-192
    • Hermeking, H.1    Benzinger, A.2
  • 31
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion G, Avruch J, (2002) 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J Biol Chem 277: 3061-3064.
    • (2002) J Biol Chem , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 32
    • 0035473486 scopus 로고    scopus 로고
    • 14-3-3 proteins; bringing new definitions to scaffolding
    • Tzivion G, Shen YH, Zhu J, (2001) 14-3-3 proteins; bringing new definitions to scaffolding. Oncogene 20: 6331-6338.
    • (2001) Oncogene , vol.20 , pp. 6331-6338
    • Tzivion, G.1    Shen, Y.H.2    Zhu, J.3
  • 33
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work?-Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe MB, (2002) How do 14-3-3 proteins work?-Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett 513: 53-57.
    • (2002) FEBS Lett , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 34
    • 27444433260 scopus 로고    scopus 로고
    • 14-3-3 proteins: regulators of numerous eukaryotic proteins
    • van Heusden GP, (2005) 14-3-3 proteins: regulators of numerous eukaryotic proteins. IUBMB Life 57: 623-629.
    • (2005) IUBMB Life , vol.57 , pp. 623-629
    • van Heusden, G.P.1
  • 35
    • 0037018148 scopus 로고    scopus 로고
    • 14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport
    • Brunet A, Kanai F, Stehn J, Xu J, Sarbassova D, et al. (2002) 14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport. J Cell Biol 156: 817-828.
    • (2002) J Cell Biol , vol.156 , pp. 817-828
    • Brunet, A.1    Kanai, F.2    Stehn, J.3    Xu, J.4    Sarbassova, D.5
  • 36
    • 2342441988 scopus 로고    scopus 로고
    • Isoform-specific differences in rapid nucleocytoplasmic shuttling cause distinct subcellular distributions of 14-3-3σ and 14-3-3ζ
    • van Hemert MJ, Niemantsverdriet M, Schmidt T, Backendorf C, Spaink HP, (2004) Isoform-specific differences in rapid nucleocytoplasmic shuttling cause distinct subcellular distributions of 14-3-3σ and 14-3-3ζ. J Cell Sci 117: 1411-1420.
    • (2004) J Cell Sci , vol.117 , pp. 1411-1420
    • van Hemert, M.J.1    Niemantsverdriet, M.2    Schmidt, T.3    Backendorf, C.4    Spaink, H.P.5
  • 37
    • 4344651089 scopus 로고    scopus 로고
    • Binding of 14-3-3beta but not 14-3-3sigma controls the cytoplasmic localization of Cdc25B: binding site preferences of 14-3-3 subtypes and the subcellular localization of Cdc25B
    • Uchida S, Kuma A, Ohtsubo M, Shimura M, Hirata M, et al. (2004) Binding of 14-3-3beta but not 14-3-3sigma controls the cytoplasmic localization of Cdc25B: binding site preferences of 14-3-3 subtypes and the subcellular localization of Cdc25B. J Cell Sci 117: 3011-3020.
    • (2004) J Cell Sci , vol.117 , pp. 3011-3020
    • Uchida, S.1    Kuma, A.2    Ohtsubo, M.3    Shimura, M.4    Hirata, M.5
  • 38
    • 0034528346 scopus 로고    scopus 로고
    • 14-3-3 proteins: regulation of subcellular localization by molecular interference
    • Muslin AJ, Xing H, (2000) 14-3-3 proteins: regulation of subcellular localization by molecular interference. Cell Signal 12: 703-709.
    • (2000) Cell Signal , vol.12 , pp. 703-709
    • Muslin, A.J.1    Xing, H.2
  • 39
    • 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, (1998) 14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts. Mol Biol Cell 9: 345-354.
    • (1998) Mol Biol Cell , vol.9 , pp. 345-354
    • Kumagai, A.1    Yakowec, P.S.2    Dunphy, W.G.3
  • 40
    • 4644262376 scopus 로고    scopus 로고
    • When the checkpoints have gone: insights into Cdc25 functional activation
    • Margolis SS, Kornbluth S, (2004) When the checkpoints have gone: insights into Cdc25 functional activation. Cell Cycle 3: 425-428.
    • (2004) Cell Cycle , vol.3 , pp. 425-428
    • Margolis, S.S.1    Kornbluth, S.2
  • 41
    • 0034594961 scopus 로고    scopus 로고
    • Specific interaction between 14-3-3 isoforms and the human Cdc25B phosphatase
    • Mils V, Baldin V, Goubin F, Pinta I, Papin C, et al. (2000) Specific interaction between 14-3-3 isoforms and the human Cdc25B phosphatase. Oncogene 19: 1257-1265.
    • (2000) Oncogene , vol.19 , pp. 1257-1265
    • Mils, V.1    Baldin, V.2    Goubin, F.3    Pinta, I.4    Papin, C.5
  • 43
    • 0035913162 scopus 로고    scopus 로고
    • Cdc25B activity is regulated by 14-3-3
    • Forrest A, Gabrielli B, (2001) Cdc25B activity is regulated by 14-3-3. Oncogene 20: 4393-4401.
    • (2001) Oncogene , vol.20 , pp. 4393-4401
    • Forrest, A.1    Gabrielli, B.2
  • 44
    • 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, (1983) Regulation of mouse oocyte meiotic maturation: implication of a decrease in oocyte cAMP and protein dephosphorylation in commitment to resume meiosis. Dev Biol 97: 264-273.
    • (1983) Dev Biol , vol.97 , pp. 264-273
    • Schultz, R.M.1    Montgomery, R.R.2    Belanoff, J.R.3
  • 45
    • 0033994867 scopus 로고    scopus 로고
    • Epigenetic modifications necessary for normal development are established during oocyte growth in mice
    • Bao S, Obata Y, Carroll J, Domeki I, Kono T, (2000) Epigenetic modifications necessary for normal development are established during oocyte growth in mice. Biol Reprod 62: 616-621.
    • (2000) Biol Reprod , vol.62 , pp. 616-621
    • Bao, S.1    Obata, Y.2    Carroll, J.3    Domeki, I.4    Kono, T.5
  • 46
    • 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, (1997) Activation of protein kinase C after fertilization is required for remodeling the mouse egg into the zygote. Mol Reprod Dev 46: 587-601.
    • (1997) Mol Reprod Dev , vol.46 , pp. 587-601
    • Gallicano, G.I.1    McGaughey, R.W.2    Capco, D.G.3


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