메뉴 건너뛰기




Volumn 1, Issue 8, 2003, Pages 589-597

The C-terminal seven amino acids in the cytoplasmic retention signal region of cyclin B2 are required for normal bipolar spindle formation in Xenopus oocytes and embryos

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYCLIN B; CYCLIN B1; CYCLIN B2; UNCLASSIFIED DRUG;

EID: 0038133462     PISSN: 15417786     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (54)
  • 1
    • 0015076873 scopus 로고
    • Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes
    • Masui, Y. and Markert, C. L. Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool., 177: 129-145, 1971.
    • (1971) J. Exp. Zool. , vol.177 , pp. 129-145
    • Masui, Y.1    Markert, C.L.2
  • 2
    • 0025246110 scopus 로고
    • Universal control mechanism regulating onset of M-phase
    • Nurse, P. Universal control mechanism regulating onset of M-phase. Nature (Lond.), 344: 503-508, 1990.
    • (1990) Nature (Lond.) , vol.344 , pp. 503-508
    • Nurse, P.1
  • 4
    • 0025736038 scopus 로고
    • Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase
    • Peter. M., Heitlinger, E., Haner, M., Aebi, U., and Nigg, E. A. Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase. EMBO J., 10: 1535-1544, 1991.
    • (1991) EMBO J. , vol.10 , pp. 1535-1544
    • Peter, M.1    Heitlinger, E.2    Haner, M.3    Aebi, U.4    Nigg, E.A.5
  • 6
    • 0026775358 scopus 로고
    • Control of microtubule dynamics and length by cyclin A- and cyclin B-dependent kinases in Xenopus egg extracts
    • Verde, F., Dogterom, M., Stelzer, E., Karsenti, E., and Leibler, S. Control of microtubule dynamics and length by cyclin A- and cyclin B-dependent kinases in Xenopus egg extracts. J. Cell Biol., 118: 1097-1108, 1992.
    • (1992) J. Cell Biol. , vol.118 , pp. 1097-1108
    • Verde, F.1    Dogterom, M.2    Stelzer, E.3    Karsenti, E.4    Leibler, S.5
  • 8
    • 0026207472 scopus 로고
    • Cyclins and their partners: From a simple idea to complicated reality
    • Hunt, T. Cyclins and their partners: from a simple idea to complicated reality. Semin. Cell Biol., 2: 213-222, 1991.
    • (1991) Semin. Cell Biol. , vol.2 , pp. 213-222
    • Hunt, T.1
  • 9
    • 0027933911 scopus 로고
    • The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B
    • Pines, J. and Hunter, T. The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B. EMBO J., 13: 3772-3781, 1994.
    • (1994) EMBO J. , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 11
    • 0024521936 scopus 로고
    • Translation of cyclin mRNA is necessary for extracts of activated Xenopus eggs to enter mitosis
    • Minshull, J., Blow, J. J., and Hunt, T. Translation of cyclin mRNA is necessary for extracts of activated Xenopus eggs to enter mitosis. Cell, 56: 947-956, 1989.
    • (1989) Cell , vol.56 , pp. 947-956
    • Minshull, J.1    Blow, J.J.2    Hunt, T.3
  • 12
    • 0026545073 scopus 로고
    • Cyclin B2 undergoes cell cycle-dependent nuclear translocation and, when expressed as a non-destructible mutant, causes mitotic arrest in HeLa cells
    • Gallant, P. and Nigg, E. A. Cyclin B2 undergoes cell cycle-dependent nuclear translocation and, when expressed as a non-destructible mutant, causes mitotic arrest in HeLa cells. J. Cell Biol., 117: 213-224, 1992.
    • (1992) J. Cell Biol. , vol.117 , pp. 213-224
    • Gallant, P.1    Nigg, E.A.2
  • 13
    • 0028123264 scopus 로고
    • Identification of a novel vertebrate cyclin: Cyclin B3 shares properties with both A- and B-type cyclins
    • Gallant, P. and Nigg, E. A. Identification of a novel vertebrate cyclin: cyclin B3 shares properties with both A- and B-type cyclins. EMBO J., 13: 595-605, 1994.
    • (1994) EMBO J. , vol.13 , pp. 595-605
    • Gallant, P.1    Nigg, E.A.2
  • 14
    • 0029019737 scopus 로고
    • Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus
    • Jackman, M., Firth, M., and Pines, J. Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus. EMBO J., 14: 1646-1654, 1995.
    • (1995) EMBO J. , vol.14 , pp. 1646-1654
    • Jackman, M.1    Firth, M.2    Pines, J.3
  • 16
    • 0026014878 scopus 로고
    • Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport
    • Pines, J. and Hunter, T. Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport. J. Cell Biol., 115: 1-17, 1991.
    • (1991) J. Cell Biol. , vol.115 , pp. 1-17
    • Pines, J.1    Hunter, T.2
  • 17
    • 0027186606 scopus 로고
    • cdc2 and its companion cyclin-dependent kinases
    • cdc2 and its companion cyclin-dependent kinases. Trends Cell Biol., 3: 296-301, 1993.
    • (1993) Trends Cell Biol. , vol.3 , pp. 296-301
    • Nigg, E.A.1
  • 18
    • 0032230190 scopus 로고    scopus 로고
    • Overexpression of the cytoplasmic retention signal region of cyclin B2, but not of cyclin B1, inhibits bipolar spindle formation in Xenopus oocytes
    • Yoshitome, S., Furuno, N., and Sagata, N. Overexpression of the cytoplasmic retention signal region of cyclin B2, but not of cyclin B1, inhibits bipolar spindle formation in Xenopus oocytes. Biol. Cell, 90: 509-518, 1998.
    • (1998) Biol. Cell , vol.90 , pp. 509-518
    • Yoshitome, S.1    Furuno, N.2    Sagata, N.3
  • 19
    • 0032525308 scopus 로고    scopus 로고
    • Nuclear export of cyclin B1 and its possible role in the DNA damage G2 checkpoint
    • Toyoshima, F., Moriguchi, T., Wada, A., Fukuda, M., and Nishida, E. Nuclear export of cyclin B1 and its possible role in the DNA damage G2 checkpoint. EMBO J., 17: 2728-2735, 1998.
    • (1998) EMBO J. , vol.17 , pp. 2728-2735
    • Toyoshima, F.1    Moriguchi, T.2    Wada, A.3    Fukuda, M.4    Nishida, E.5
  • 20
    • 0032528290 scopus 로고    scopus 로고
    • MPF localization is controlled by nuclear export
    • Hagting, A., Karlsson, C., Clute, P., Jackman, M., and Pines, J. MPF localization is controlled by nuclear export. EMBO J., 17: 4127-4138, 1998.
    • (1998) EMBO J. , vol.17 , pp. 4127-4138
    • Hagting, A.1    Karlsson, C.2    Clute, P.3    Jackman, M.4    Pines, J.5
  • 21
    • 0032528001 scopus 로고    scopus 로고
    • Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1
    • Yang, J., Bardes, E. S., Moore, J. D., Brennan, J., Powers, M. A., and Kornbluth, S. Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1. Genes Dev., 12: 2131-2143, 1998.
    • (1998) Genes Dev. , vol.12 , pp. 2131-2143
    • Yang, J.1    Bardes, E.S.2    Moore, J.D.3    Brennan, J.4    Powers, M.A.5    Kornbluth, S.6
  • 22
    • 0033166064 scopus 로고    scopus 로고
    • Translocation of cyclin B1 to the nucleus at prophase requires a phosphorylation-dependent nuclear import signal
    • Hagting, A., Jackman, M., Simpson, K., and Pines, J. Translocation of cyclin B1 to the nucleus at prophase requires a phosphorylation-dependent nuclear import signal. Curr. Biol. 9: 680-689, 1999.
    • (1999) Curr. Biol. , vol.9 , pp. 680-689
    • Hagting, A.1    Jackman, M.2    Simpson, K.3    Pines, J.4
  • 23
    • 0031028382 scopus 로고    scopus 로고
    • Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation
    • Li, J., Meyer, A. N., and Donoghue, D. J. Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation. Proc. Natl. Acad. Sci. USA, 94: 502-507, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 502-507
    • Li, J.1    Meyer, A.N.2    Donoghue, D.J.3
  • 24
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., Ohno, M., Yoshida, M., and Mattaj, I. W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell, 90: 1051-1060, 1997.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 26
    • 0025874692 scopus 로고
    • On the synthesis and destruction of A- and B-type cyclins during oogenesis and meiotic maturation in Xenopus laevis
    • Kobayashi, H., Minshull, J., Ford, C., Golsteyn, R., Poon, R., and Hunt, T. On the synthesis and destruction of A- and B-type cyclins during oogenesis and meiotic maturation in Xenopus laevis. J. Cell Biol., 114: 755-765, 1991.
    • (1991) J. Cell Biol. , vol.114 , pp. 755-765
    • Kobayashi, H.1    Minshull, J.2    Ford, C.3    Golsteyn, R.4    Poon, R.5    Hunt, T.6
  • 27
    • 0029053823 scopus 로고
    • Chromosomes take the lead in spindle assembly
    • Vernos, I. and Karsenti, E. Chromosomes take the lead in spindle assembly. Trends Cell Biol., 5: 297-301, 1995.
    • (1995) Trends Cell Biol. , vol.5 , pp. 297-301
    • Vernos, I.1    Karsenti, E.2
  • 28
    • 0030883130 scopus 로고    scopus 로고
    • Pathways of spindle pole formation: Different mechanisms; conserved components
    • Merdes, A. and Cleveland, D. W. Pathways of spindle pole formation: different mechanisms; conserved components. J. Cell Biol., 138: 953-956, 1997.
    • (1997) J. Cell Biol. , vol.138 , pp. 953-956
    • Merdes, A.1    Cleveland, D.W.2
  • 29
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer, U., Huber, J., Boelens, W. C., Mattaj, I. W., and Luhrmann, R. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell, 82: 475-483, 1995.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Luhrmann, R.5
  • 30
    • 0032728975 scopus 로고    scopus 로고
    • Human cyclin A is required for mitosis until mid prophase
    • Furuno, N., den Elzen, N., and Pines, J. Human cyclin A is required for mitosis until mid prophase. J. Cell Biol., 147: 295-306, 1999.
    • (1999) J. Cell Biol. , vol.147 , pp. 295-306
    • Furuno, N.1    Den Elzen, N.2    Pines, J.3
  • 31
    • 0033601783 scopus 로고    scopus 로고
    • Nuclear import of Cdk/cyclin complexes: Identification of distinct mechanisms for import of Cdk2/cyclin E and Cdc2/cyclin B1
    • Moore, J. D., Yang, J., Truant, R., and Kornbluth, S. Nuclear import of Cdk/cyclin complexes: identification of distinct mechanisms for import of Cdk2/cyclin E and Cdc2/cyclin B1. J. Cell Biol., 144: 213-224, 1999.
    • (1999) J. Cell Biol. , vol.144 , pp. 213-224
    • Moore, J.D.1    Yang, J.2    Truant, R.3    Kornbluth, S.4
  • 32
    • 0035162304 scopus 로고    scopus 로고
    • Cytoplasmic occurrence of the Chk1/Cdc25 pathway and regulation of Chk1 in Xenopus oocytes
    • Oe, T., Nakajo, N., Katsuragi, Y., Okazaki, K., and Sagata, N. Cytoplasmic occurrence of the Chk1/Cdc25 pathway and regulation of Chk1 in Xenopus oocytes. Dev. Biol., 229: 250-261, 2001.
    • (2001) Dev. Biol. , vol.229 , pp. 250-261
    • Oe, T.1    Nakajo, N.2    Katsuragi, Y.3    Okazaki, K.4    Sagata, N.5
  • 33
    • 0035029388 scopus 로고    scopus 로고
    • Requirement of cyclin B2, but not cyclin B1, for bipolar spindle formation in frog (Rana japonica) oocytes
    • Kotani, T., Yoshida, N., Mita, K., and Yamashita, M. Requirement of cyclin B2, but not cyclin B1, for bipolar spindle formation in frog (Rana japonica) oocytes. Mol. Reprod. Dev., 59: 199-208, 2001.
    • (2001) Mol. Reprod. Dev. , vol.59 , pp. 199-208
    • Kotani, T.1    Yoshida, N.2    Mita, K.3    Yamashita, M.4
  • 35
    • 0022919318 scopus 로고
    • Beyond self-assembly: From microtubules to morphogenesis
    • Kirschner, M. and Mitchison, T. Beyond self-assembly: from microtubules to morphogenesis. Cell, 45: 329-342, 1986.
    • (1986) Cell , vol.45 , pp. 329-342
    • Kirschner, M.1    Mitchison, T.2
  • 37
    • 0029836330 scopus 로고    scopus 로고
    • Self-organization of microtubules into bipolar spindles around artificial chromosomes in Xenopus egg extracts
    • Heald, R., Tournebize, R., Blank, T., Sandaltzopoulos, R., Becker, P., Hyman, A., and Karsenti, E. Self-organization of microtubules into bipolar spindles around artificial chromosomes in Xenopus egg extracts. Nature (Lond.), 382: 420-425, 1996.
    • (1996) Nature (Lond.) , vol.382 , pp. 420-425
    • Heald, R.1    Tournebize, R.2    Blank, T.3    Sandaltzopoulos, R.4    Becker, P.5    Hyman, A.6    Karsenti, E.7
  • 38
    • 0029417238 scopus 로고
    • cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo
    • cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo. Cell, 83: 1159-1169, 1995.
    • (1995) Cell , vol.83 , pp. 1159-1169
    • Blangy, A.1    Lane, H.A.2    D'Herin, P.3    Harper, M.4    Kress, M.5    Nigg, E.A.6
  • 39
    • 0029011952 scopus 로고
    • Mutations in the kinesin-like protein Eg5 disrupting localization to the mitotic spindle
    • Sawin, K. E. and Mitchison, T. J. Mutations in the kinesin-like protein Eg5 disrupting localization to the mitotic spindle. Proc. Natl. Acad. Sci. USA, 92: 4289-4293, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4289-4293
    • Sawin, K.E.1    Mitchison, T.J.2
  • 41
    • 0030070110 scopus 로고    scopus 로고
    • Xklp2, a novel Xenopus centrosomal kinesin-like protein required for centrosome separation during mitosis
    • Boleti, H., Karsenti, E., and Vernos, I. Xklp2, a novel Xenopus centrosomal kinesin-like protein required for centrosome separation during mitosis. Cell, 84: 49-59, 1996.
    • (1996) Cell , vol.84 , pp. 49-59
    • Boleti, H.1    Karsenti, E.2    Vernos, I.3
  • 42
    • 0026087534 scopus 로고
    • Organization, nucleation, and acetylation of microtubules in Xenopus laevis oocytes: A study by confocal immunofluorescence microscopy
    • Gard, D. L. Organization, nucleation, and acetylation of microtubules in Xenopus laevis oocytes: a study by confocal immunofluorescence microscopy. Dev. Biol., 143: 346-362, 1991.
    • (1991) Dev. Biol. , vol.143 , pp. 346-362
    • Gard, D.L.1
  • 43
    • 0026717165 scopus 로고
    • Microtubule organization during maturation of Xenopus oocytes: Assembly and rotation of the meiotic spindles
    • Gard, D. L. Microtubule organization during maturation of Xenopus oocytes: assembly and rotation of the meiotic spindles. Dev. Biol., 151: 516-530, 1992.
    • (1992) Dev. Biol. , vol.151 , pp. 516-530
    • Gard, D.L.1
  • 44
    • 0033055061 scopus 로고    scopus 로고
    • Cyclin-dependent kinase control of centrosome duplication
    • Lacey, K. R., Jackson, P. K., and Stearns, T. Cyclin-dependent kinase control of centrosome duplication. Proc. Natl. Acad. Sci. USA, 96: 2817-2822, 1999.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2817-2822
    • Lacey, K.R.1    Jackson, P.K.2    Stearns, T.3
  • 45
    • 0026739078 scopus 로고
    • Mitotic spindle organization by a plus-end-directed microtubule motor
    • Sawin, K. E., LeGuellec, K., Philippe, M., and Mitchison, T. J. Mitotic spindle organization by a plus-end-directed microtubule motor. Nature (Lond.), 359: 540-543, 1992.
    • (1992) Nature (Lond.) , vol.359 , pp. 540-543
    • Sawin, K.E.1    LeGuellec, K.2    Philippe, M.3    Mitchison, T.J.4
  • 46
    • 13144251122 scopus 로고    scopus 로고
    • A model for the proposed roles of different microtubule-based motor proteins in establishing spindle bipolarity
    • Walczak, C. E., Vernos, I., Mitchison, T. J., Karsenti, E., and Heald, R. A. model for the proposed roles of different microtubule-based motor proteins in establishing spindle bipolarity. Curr. Biol., 8: 903-913, 1998.
    • (1998) Curr. Biol. , vol.8 , pp. 903-913
    • Walczak, C.E.1    Vernos, I.2    Mitchison, T.J.3    Karsenti, E.4    Heald, R.5
  • 47
    • 0024280269 scopus 로고
    • Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes
    • Sagata, N., Oskarsson, M., Copeland, T., Brumbaugh, J., and Vande Woude, G. F. Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes. Nature (Lond.), 335: 519-525, 1988.
    • (1988) Nature (Lond.) , vol.335 , pp. 519-525
    • Sagata, N.1    Oskarsson, M.2    Copeland, T.3    Brumbaugh, J.4    Vande Woude, G.F.5
  • 48
    • 0028338959 scopus 로고
    • Suppression of DNA replication via Mos function during meiotic divisions in Xenopus oocytes
    • Furuno, N., Nishizawa, M., Okazaki, K., Tanaka, H., Iwashita, J., Nakajo, N. Ogawa, Y., and Sagata, N. Suppression of DNA replication via Mos function during meiotic divisions in Xenopus oocytes. EMBO J., 13: 2399-2410, 1994.
    • (1994) EMBO J. , vol.13 , pp. 2399-2410
    • Furuno, N.1    Nishizawa, M.2    Okazaki, K.3    Tanaka, H.4    Iwashita, J.5    Nakajo, N.6    Ogawa, Y.7    Sagata, N.8
  • 49
    • 0015292069 scopus 로고
    • Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals
    • Dumont, J. N. Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals. J. Morphol., 136: 153-179, 1972.
    • (1972) J. Morphol. , vol.136 , pp. 153-179
    • Dumont, J.N.1
  • 50
    • 0026794460 scopus 로고
    • The oocyte nucleus isolated in oil retains in vivo structure and functions
    • Paine, P. L., Johnson, M. E., Lau, Y. T., Tluczek, L. J. M., and Miller, D. S. The oocyte nucleus isolated in oil retains in vivo structure and functions. Biotechniques, 13: 238-246, 1992.
    • (1992) Biotechniques , vol.13 , pp. 238-246
    • Paine, P.L.1    Johnson, M.E.2    Lau, Y.T.3    Tluczek, L.J.M.4    Miller, D.S.5
  • 53
    • 0025012866 scopus 로고
    • Cyclin is a component of maturation-promoting factor from Xenopus
    • Gautier, J., Minshull, J., Lohka, M., Glotzer, M., Hunt, T., and Maller, J. L. Cyclin is a component of maturation-promoting factor from Xenopus. Cell, 60: 487-494, 1990.
    • (1990) Cell , vol.60 , pp. 487-494
    • Gautier, J.1    Minshull, J.2    Lohka, M.3    Glotzer, M.4    Hunt, T.5    Maller, J.L.6
  • 54
    • 0026751110 scopus 로고
    • The "second-codon rule" and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in Xenopus oocytes
    • Nishizawa, M., Okazaki, K., Furuno, N., Watanabe, N., and Sagata, N. The "second-codon rule" and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in Xenopus oocytes. EMBO J., 11: 2433-2446, 1992.
    • (1992) EMBO J. , vol.11 , pp. 2433-2446
    • Nishizawa, M.1    Okazaki, K.2    Furuno, N.3    Watanabe, N.4    Sagata, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.