메뉴 건너뛰기




Volumn 111, Issue 12, 1998, Pages 1751-1757

The Polo-like kinase Plx1 is a component of the MPF amplification loop at the G2/M-phase transition of the cell cycle in Xenopus eggs

Author keywords

Mitosis; MPF amplification; Polo kinase; Xenopus egg

Indexed keywords

CYCLIN A; CYCLIN B; PROTEIN KINASE;

EID: 0031850551     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (181)

References (43)
  • 1
    • 0030051121 scopus 로고    scopus 로고
    • MAP kinase does not inactivate, but rather prevents the cyclin degradation pathway from being turned on in Xenopus egg extracts
    • Abrieu, A., Lorca, T., Labbé, J. C., Morin, N., Keyse, S. and Dorée, M. (1996). MAP kinase does not inactivate, but rather prevents the cyclin degradation pathway from being turned on in Xenopus egg extracts, J. Cell Sci. 109, 239-246.
    • (1996) J. Cell Sci. , vol.109 , pp. 239-246
    • Abrieu, A.1    Lorca, T.2    Labbé, J.C.3    Morin, N.4    Keyse, S.5    Dorée, M.6
  • 3
    • 0031203337 scopus 로고    scopus 로고
    • Why do protein kinase cascades have more than one level
    • Brown, G. C., Hoek, J. B. and Kholodenko, B. N. (1997). Why do protein kinase cascades have more than one level. Trends Biochem. Sci. 22, 288.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 288
    • Brown, G.C.1    Hoek, J.B.2    Kholodenko, B.N.3
  • 4
    • 0026506719 scopus 로고
    • Cyclin A- and cyclin B-dependent protein kinases are regulated by different mechanisms in Xenopus egg extracts
    • Clarke, P. R., Leiss, D., Pagano, M. and Karsenti, E. (1992). Cyclin A- and cyclin B-dependent protein kinases are regulated by different mechanisms in Xenopus egg extracts. EMBO J. 11, 1751-1761.
    • (1992) EMBO J. , vol.11 , pp. 1751-1761
    • Clarke, P.R.1    Leiss, D.2    Pagano, M.3    Karsenti, E.4
  • 6
    • 0026674074 scopus 로고
    • Cyclin A potentiates maturation-promoting factor activation in the early Xenopus embryo via inhibition of the tyrosine kinase that phosphorylates cdc2
    • Devault, A., Fesquet, D., Cavadore, J. C., Garrigues, A. M., Labbé, J. C., Lorca, T., Picard, A., Philippe, M. and Dorée, M. (1992). Cyclin A potentiates maturation-promoting factor activation in the early Xenopus embryo via inhibition of the tyrosine kinase that phosphorylates cdc2. J. Cell Biol. 118, 1109-1120.
    • (1992) J. Cell Biol. , vol.118 , pp. 1109-1120
    • Devault, A.1    Fesquet, D.2    Cavadore, J.C.3    Garrigues, A.M.4    Labbé, J.C.5    Lorca, T.6    Picard, A.7    Philippe, M.8    Dorée, M.9
  • 7
    • 0025288876 scopus 로고
    • Control of M-phase by maturation-promoting factor
    • Dorée, M. (1990). Control of M-phase by maturation-promoting factor. Curr. Opin. Cell Biol. 2, 269-273.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 269-273
    • Dorée, M.1
  • 8
    • 0025938467 scopus 로고
    • The cdc25 protein contains an intrinsic phosphatase activity
    • Dunphy, W. G. and Kumagai, A. (1991). The cdc25 protein contains an intrinsic phosphatase activity. Cell 67, 189-196.
    • (1991) Cell , vol.67 , pp. 189-196
    • Dunphy, W.G.1    Kumagai, A.2
  • 9
    • 0027280212 scopus 로고
    • A conserved mitotic kinase active at late anaphase-telophase in syncytical Drosophila embryos
    • Fenton, B. and Glover, D. M. (1931). A conserved mitotic kinase active at late anaphase-telophase in syncytical Drosophila embryos. Nature 363, 637-640.
    • (1931) Nature , vol.363 , pp. 637-640
    • Fenton, B.1    Glover, D.M.2
  • 10
    • 0030445778 scopus 로고    scopus 로고
    • Tripping the switch fantastic: How a protein kinase cascade can convert graded inputs into switch-like outputs
    • Ferrell, J. E. Jr (1996). Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs. Trends Biochem. Sci. 21, 460-466.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 460-466
    • Ferrell Jr., J.E.1
  • 11
    • 0031203921 scopus 로고    scopus 로고
    • How responses get more switch-like as you move down a protein kinase cascade
    • Ferrell, J. E. Jr (1997). How responses get more switch-like as you move down a protein kinase cascade. Trends Biochem. Sci. 22, 288-289.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 288-289
    • Ferrell Jr., J.E.1
  • 13
    • 0030447434 scopus 로고    scopus 로고
    • Polo kinase: The choreographer of the mitotic stages?
    • GJlover, D. M., Ohkura, H. and Tavares, A. (1996). Polo kinase: the choreographer of the mitotic stages? Cell Biol. 135, 1681-1684.
    • (1996) Cell Biol. , vol.135 , pp. 1681-1684
    • Glover, D.M.1    Ohkura, H.2    Tavares, A.3
  • 14
    • 0029079267 scopus 로고
    • Cell cycle regulation of the activity and subcellular localization of PLKL a human protein kinase implicated in mitotic spindle function
    • Golsteyn, R. M., Mundt, K. E., Fry, A. M. and Nigg, E. A. (1995). Cell cycle regulation of the activity and subcellular localization of PLKL a human protein kinase implicated in mitotic spindle function. J. Cell Biol. 129, 1617-1628.
    • (1995) J. Cell Biol. , vol.129 , pp. 1617-1628
    • Golsteyn, R.M.1    Mundt, K.E.2    Fry, A.M.3    Nigg, E.A.4
  • 16
    • 0027509501 scopus 로고
    • Phosphorylation and activation of human cdc25-C by cdc2-cyclin B and its involvement in the self-amplification of MPF- at mitosis
    • Hoffmann, I., Clarke, P. R., Marcote, M. J., Karsenti, K. and Draetta, G. (1993). Phosphorylation and activation of human cdc25-C by cdc2-cyclin B and its involvement in the self-amplification of MPF- at mitosis. EMBO J. 12, 53-63.
    • (1993) EMBO J. , vol.12 , pp. 53-63
    • Hoffmann, I.1    Clarke, P.R.2    Marcote, M.J.3    Karsenti, K.4    Draetta, G.5
  • 17
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogen-activated protein kinase cascade
    • Huang, C. Y. and Ferrell, J. E. Jr (1996). Ultrasensitivity in the mitogen-activated protein kinase cascade. Proc. Nat. Acad. Sci. USA 93, 10078-10083.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 10078-10083
    • Huang, C.Y.1    Ferrell Jr., J.E.2
  • 18
    • 0027746003 scopus 로고
    • Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase
    • Izumi, T. and Maller, J. L. (1993). Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase. Mol. Biol. Cell 4, 1337-1350.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1337-1350
    • Izumi, T.1    Maller, J.L.2
  • 19
    • 0026580389 scopus 로고
    • Oscillation of MPF is accompanied by periodic association between cdc25 and cdc2-cyclin B
    • Jessus, C. and Beach, D. (1992). Oscillation of MPF is accompanied by periodic association between cdc25 and cdc2-cyclin B. Cell 68, 323-332.
    • (1992) Cell , vol.68 , pp. 323-332
    • Jessus, C.1    Beach, D.2
  • 22
    • 0026580389 scopus 로고
    • Oscillation of MPF is accompanied by periodical association between cdc25 and cdc2-csclin B
    • Kumagai, A. and Dunphy, W. G. (1992). Oscillation of MPF is accompanied by periodical association between cdc25 and cdc2-csclin B. Cell 68, 323-332.
    • (1992) Cell , vol.68 , pp. 323-332
    • Kumagai, A.1    Dunphy, W.G.2
  • 23
    • 0029821131 scopus 로고    scopus 로고
    • Purification and molecular cloning of Plxl. a cdc25 regulatory, kinase from Xenopus egg extracts
    • Kumagai, A. and Dunphy, W. G. (1996). Purification and molecular cloning of Plxl. a cdc25 regulatory, kinase from Xenopus egg extracts. Science 273, 1377-1380
    • (1996) Science , vol.273 , pp. 1377-1380
    • Kumagai, A.1    Dunphy, W.G.2
  • 24
    • 0026334431 scopus 로고
    • M-phase specific cdc2 kinase: Preparation from starfish and properties
    • Labbé, J. C., Cavadore, J. C. and Dorée, M. (1991). M-phase specific cdc2 kinase: preparation from starfish and properties. Meth. Enzymol. 201, 291-301.
    • (1991) Meth. Enzymol. , vol.201 , pp. 291-301
    • Labbé, J.C.1    Cavadore, J.C.2    Dorée, M.3
  • 25
    • 0031081209 scopus 로고    scopus 로고
    • Cell-cycle control Polo-like kinases join the outer circle
    • Lane, H. A. and Nigg, E. A. (1997). Cell-cycle control Polo-like kinases join the outer circle. Trends Cell Biol. 7, 63-68.
    • (1997) Trends Cell Biol. , vol.7 , pp. 63-68
    • Lane, H.A.1    Nigg, E.A.2
  • 26
    • 0030924977 scopus 로고    scopus 로고
    • Plk is a functional homolog of Saccharomyces cerevisiae cdc5. and elevated Plk activity induces multiple septation structures
    • Lee, K. S. and Erikson, R. L. (1997). Plk is a functional homolog of Saccharomyces cerevisiae cdc5. and elevated Plk activity induces multiple septation structures. Mol. Cell Biol. 17, 3408-3417.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 3408-3417
    • Lee, K.S.1    Erikson, R.L.2
  • 29
    • 0015076873 scopus 로고
    • Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes
    • Masui, Y. and Markert, C. L. (1971). Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool. 177, 129-145.
    • (1971) J. Exp. Zool. , vol.177 , pp. 129-145
    • Masui, Y.1    Markert, C.L.2
  • 30
    • 0028059515 scopus 로고
    • The proteolysis-dependent metaphase to anaphase transition: Calcium/calmodulin-dependem protein kinase II mediates onset of anaphase in extracts prepared from unfertilized Xenopus eggs
    • Morin, N., Abrieu, A., Lorca, T., Martin, F. and Dorée, M. (1994). The proteolysis-dependent metaphase to anaphase transition: calcium/calmodulin-dependem protein kinase II mediates onset of anaphase in extracts prepared from unfertilized Xenopus eggs. EMBO J. 13, 4343-4352.
    • (1994) EMBO J. , vol.13 , pp. 4343-4352
    • Morin, N.1    Abrieu, A.2    Lorca, T.3    Martin, F.4    Dorée, M.5
  • 31
    • 0028998865 scopus 로고
    • Cell cycle regulation of a Xenopus weel-like kinase Mol
    • Mueller, P. R., Coleman, T. R. and Dunphy, W. G. (1995a). Cell cycle regulation of a Xenopus weel-like kinase Mol. Biol. Cell 6, 119-134.
    • (1995) Biol. Cell , vol.6 , pp. 119-134
    • Mueller, P.R.1    Coleman, T.R.2    Dunphy, W.G.3
  • 32
    • 0028783413 scopus 로고
    • MYT I: A membrane-associated inhibitory kinase that phosphorylates cdc2 on both threonine 14 and tyrosine 15
    • Mueller, P. R., Coleman, T. R. and Dunphy, W. G. (1995b). MYT I: a membrane-associated inhibitory kinase that phosphorylates cdc2 on both threonine 14 and tyrosine 15. Science 270, 86-90.
    • (1995) Science , vol.270 , pp. 86-90
    • Mueller, P.R.1    Coleman, T.R.2    Dunphy, W.G.3
  • 33
    • 0024978338 scopus 로고
    • Cyclin synthesis drives the early embryonic cell cycle
    • Murray, A. W. and Kirschner, M. W. (1989). Cyclin synthesis drives the early embryonic cell cycle. Nature 339, 275-280.
    • (1989) Nature , vol.339 , pp. 275-280
    • Murray, A.W.1    Kirschner, M.W.2
  • 34
    • 0025246110 scopus 로고
    • Universal control mechanism regulating onset of M-phase
    • Nurse, P. (1990). Universal control mechanism regulating onset of M-phase. Nature 344, 503-508.
    • (1990) Nature , vol.344 , pp. 503-508
    • Nurse, P.1
  • 36
    • 0022462146 scopus 로고
    • + functions as an inducer in the mitotic control of fission yeast
    • + functions as an inducer in the mitotic control of fission yeast. Cell 45, 145-153.
    • (1986) Cell , vol.45 , pp. 145-153
    • Russell, P.1    Nurse, P.2
  • 38
    • 0023804548 scopus 로고
    • Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles
    • Sunkel, C. K. and Glover, D. M. (1988). Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles. J. Cell Sci. 89, 25-38.
    • (1988) J. Cell Sci. , vol.89 , pp. 25-38
    • Sunkel, C.K.1    Glover, D.M.2
  • 41
    • 0029838630 scopus 로고    scopus 로고
    • The conserved mitotic kinase Polo is regulated by phosphorylation and has preferred microtubule-associated substrates in Drosophila embryo extracts
    • Tavares, A. A., Glover, D. M. and Sunkel, C. E. (1996). The conserved mitotic kinase Polo is regulated by phosphorylation and has preferred microtubule-associated substrates in Drosophila embryo extracts. EMBO J. 15, 4873-4883.
    • (1996) EMBO J. , vol.15 , pp. 4873-4883
    • Tavares, A.A.1    Glover, D.M.2    Sunkel, C.E.3
  • 42
    • 0030613751 scopus 로고    scopus 로고
    • 2- phase arrest in Xenopus egg extracts by activation of p42 mitogen-activated protein kinase
    • 2- phase arrest in Xenopus egg extracts by activation of p42 mitogen-activated protein kinase. Mol. Biol. Cell 8, 2157-2169.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2157-2169
    • Walter, S.A.1    Guadagno, T.M.2    Ferrell, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.