메뉴 건너뛰기




Volumn 254, Issue 2, 2000, Pages 249-256

The Xenopus XMAP215 and its human homologue TOG proteins interact with cyclin B1 to target p34cdc2 to microtubules during mitosis

Author keywords

Mitosis, microtubules; p34cdc2 cyclin B1; XMAP215 TOGp

Indexed keywords

CYCLIN B1; MATURATION PROMOTING FACTOR; MICROTUBULE ASSOCIATED PROTEIN; PROTEIN KINASE; TOG PROTEIN; UNCLASSIFIED DRUG; XMAP 215 PROTEIN;

EID: 0034141716     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4740     Document Type: Article
Times cited : (40)

References (44)
  • 1
    • 0025246110 scopus 로고
    • Universal control mechanism regulating onset of M-phase
    • Nurse P. Universal control mechanism regulating onset of M-phase. Nature. 344:1990;503-508.
    • (1990) Nature , vol.344 , pp. 503-508
    • Nurse, P.1
  • 2
    • 0025288876 scopus 로고
    • Control of M-phase by maturation-promoting factor
    • Doree M. Control of M-phase by maturation-promoting factor. Curr. Opin. Cell. Biol. 2:1990;269-273.
    • (1990) Curr. Opin. Cell. Biol. , vol.2 , pp. 269-273
    • Doree, M.1
  • 3
    • 0026207472 scopus 로고
    • Cyclins and their partners: From a simple idea to complex reality
    • Hunt T. Cyclins and their partners: from a simple idea to complex reality. Semin. Cell. Biol. 2:1991;213-222.
    • (1991) Semin. Cell. Biol. , vol.2 , pp. 213-222
    • Hunt, T.1
  • 4
    • 0029317904 scopus 로고
    • Cyclin-dependent protein kinases: Key regulators of the eucaryotic cell cycle
    • Nigg E. A. Cyclin-dependent protein kinases: key regulators of the eucaryotic cell cycle. Bioassays. 17:1995;471-480.
    • (1995) Bioassays , vol.17 , pp. 471-480
    • Nigg, E.A.1
  • 5
    • 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., Pines J. Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus. EMBO J. 14:1995;1646-1654.
    • (1995) EMBO J. , vol.14 , pp. 1646-1654
    • Jackman, M.1    Firth, M.2    Pines, J.3
  • 6
    • 0025572606 scopus 로고
    • P34cdc2 kinase is locolized to distincts domains within the mitotic apparatus
    • Rattner J. B., Lew J., Wang J. H. p34cdc2 kinase is locolized to distincts domains within the mitotic apparatus. Cell. Motil. Cytoskeleton. 17:1990;227-235.
    • (1990) Cell. Motil. Cytoskeleton. , vol.17 , pp. 227-235
    • Rattner, J.B.1    Lew, J.2    Wang, J.H.3
  • 7
    • 0026014878 scopus 로고
    • Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport
    • Pines J., Hunter T. Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport. J. Cell. Biol. 115:1991;1-17.
    • (1991) J. Cell. Biol. , vol.115 , pp. 1-17
    • Pines, J.1    Hunter, T.2
  • 8
    • 0026580551 scopus 로고
    • Cyclins A and B associate with chromatin and polar regions of spindles, respectively, and do not undergo complete degradation at anaphase in syncytial Drosophila embryos
    • Maldonado-Codina G., Glover D. M. Cyclins A and B associate with chromatin and polar regions of spindles, respectively, and do not undergo complete degradation at anaphase in syncytial Drosophila embryos. J. Cell. Biol. 116:1992;967-976.
    • (1992) J. Cell. Biol. , vol.116 , pp. 967-976
    • Maldonado-Codina, G.1    Glover, D.M.2
  • 9
    • 0026568213 scopus 로고
    • Relocation and distinct subcellular localization of p34cdc2-cyclin B complex at meiosis reinitiation in starfish oocytes
    • Ookata K., Hisanaga S., Okano T., Tachibana K., Kishimoto T. Relocation and distinct subcellular localization of p34cdc2-cyclin B complex at meiosis reinitiation in starfish oocytes. EMBO J. 11:1992;1763-1772.
    • (1992) EMBO J. , vol.11 , pp. 1763-1772
    • Ookata, K.1    Hisanaga, S.2    Okano, T.3    Tachibana, K.4    Kishimoto, T.5
  • 10
    • 0024786266 scopus 로고
    • P34cdc2 is located in both nucleus and cytoplasm; Part is centrosomally associated at G2/M and enters vesicles at anaphase
    • Bailly E., Doree M., Nurse P., Bornens M. p34cdc2 is located in both nucleus and cytoplasm; part is centrosomally associated at G2/M and enters vesicles at anaphase. EMBO J. 8:1989;3985-3995.
    • (1989) EMBO J. , vol.8 , pp. 3985-3995
    • Bailly, E.1    Doree, M.2    Nurse, P.3    Bornens, M.4
  • 11
    • 0026603096 scopus 로고
    • Cytoplasmic accumulation of cyclin B1 in human cells: Association with a detergent-resistant compartment and with the centrosome
    • Bailly E., Pines J., Hunter T., Bornens M. Cytoplasmic accumulation of cyclin B1 in human cells: Association with a detergent-resistant compartment and with the centrosome. J. Cell Sci. 101:1992;529-545.
    • (1992) J. Cell Sci. , vol.101 , pp. 529-545
    • Bailly, E.1    Pines, J.2    Hunter, T.3    Bornens, M.4
  • 12
    • 0028927505 scopus 로고
    • Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics
    • Ookata K., Hisanaga S., Bulinski J. C., Murofushi H., Aizawa H., Itoh T. J., Hotani H., Okumura E., Tachibana K., Kishimoto T. Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics. J. Cell. Biol. 128:1995;849-862.
    • (1995) J. Cell. Biol. , vol.128 , pp. 849-862
    • Ookata, K.1    Hisanaga, S.2    Bulinski, J.C.3    Murofushi, H.4    Aizawa, H.5    Itoh, T.J.6    Hotani, H.7    Okumura, E.8    Tachibana, K.9    Kishimoto, T.10
  • 13
    • 0027085694 scopus 로고
    • Microtubule stabilisation by assembly-promoting microtubule-associated proteins: A repeat performance
    • Chapin S. J., Bulinski J. C. Microtubule stabilisation by assembly-promoting microtubule-associated proteins: A repeat performance. Cell Motil. Cytoskeleton. 23:1992;236-243.
    • (1992) Cell Motil. Cytoskeleton , vol.23 , pp. 236-243
    • Chapin, S.J.1    Bulinski, J.C.2
  • 14
    • 0022850973 scopus 로고
    • Microtubule-associated proteins
    • Olmsted J. B. Microtubule-associated proteins. Annu. Rev. Cell. Biol. 2:1986;421-457.
    • (1986) Annu. Rev. Cell. Biol. , vol.2 , pp. 421-457
    • Olmsted, J.B.1
  • 15
    • 0025303594 scopus 로고
    • Molecular characterization of high molecular weight microtubule-associated proteins: Some answers, many questions
    • Vallee R. B. Molecular characterization of high molecular weight microtubule-associated proteins: Some answers, many questions. Cell. Motil. Cytoskeleton. 15:1990;204-209.
    • (1990) Cell. Motil. Cytoskeleton. , vol.15 , pp. 204-209
    • Vallee, R.B.1
  • 16
    • 0028823831 scopus 로고
    • Characterization of the cDNA and pattern of expression of a new gene over-expressed in human hepatomas and colonic tumors
    • Charrasse S., Mazel M., Taviaux S., Berta P., Chow T., Larroque C. Characterization of the cDNA and pattern of expression of a new gene over-expressed in human hepatomas and colonic tumors. Eur. J. Biochem. 234:1995;406-413.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 406-413
    • Charrasse, S.1    Mazel, M.2    Taviaux, S.3    Berta, P.4    Chow, T.5    Larroque, C.6
  • 17
    • 0023589342 scopus 로고
    • A microtubule-associated protein from Xenopus eggs that specifically promotes assembly at the plus-end
    • Gard D. L., Kirschner M. W. A microtubule-associated protein from Xenopus eggs that specifically promotes assembly at the plus-end. J. Cell. Biol. 105:1987;2203-2215.
    • (1987) J. Cell. Biol. , vol.105 , pp. 2203-2215
    • Gard, D.L.1    Kirschner, M.W.2
  • 19
    • 0027372852 scopus 로고
    • Regulation of microtubule dynamic instability
    • Cassimeris L. Regulation of microtubule dynamic instability. Cell Motil. Cytoskeleton. 26:1993;275-281.
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 275-281
    • Cassimeris, L.1
  • 20
    • 0027239819 scopus 로고
    • Association of p34cdc2/cyclin B complex with microtubules in starfish oocytes
    • Ookata K., Hisanaga S., Okumura E., Kishimoto T. Association of p34cdc2/cyclin B complex with microtubules in starfish oocytes. J. Cell Sci. 105:1993;873-881.
    • (1993) J. Cell Sci. , vol.105 , pp. 873-881
    • Ookata, K.1    Hisanaga, S.2    Okumura, E.3    Kishimoto, T.4
  • 21
    • 0022960026 scopus 로고
    • Purification of tau protein from brain
    • Drubin D., Kirschner M. Purification of tau protein from brain. Methods Enzymol. 134:1986;156-160.
    • (1986) Methods Enzymol. , vol.134 , pp. 156-160
    • Drubin, D.1    Kirschner, M.2
  • 22
    • 0020031810 scopus 로고
    • A taxol-dependent procedure for the isolation of microtubules and microtubule-associated proteins (MAPs)
    • Vallee R. B. A taxol-dependent procedure for the isolation of microtubules and microtubule-associated proteins (MAPs). J. Cell. Biol. 92:1982;435-442.
    • (1982) J. Cell. Biol. , vol.92 , pp. 435-442
    • Vallee, R.B.1
  • 23
    • 0020841301 scopus 로고
    • Isolation of sea urchin egg microtubules with taxol and identification of mitotic spindle microtubule-associated proteins with monoclonal antibodies
    • Vallee R. B., Bloom G. S. Isolation of sea urchin egg microtubules with taxol and identification of mitotic spindle microtubule-associated proteins with monoclonal antibodies. Proc. Natl. Acad. Sci. USA. 80:1983;6259-6263.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6259-6263
    • Vallee, R.B.1    Bloom, G.S.2
  • 25
    • 0025821565 scopus 로고
    • Cyclin B targets p34cdc2 for tyrosine phosphorylation
    • Meijer L., Azzi L., Wang J. Y. Cyclin B targets p34cdc2 for tyrosine phosphorylation. EMBO J. 10:1991;1545-1554.
    • (1991) EMBO J. , vol.10 , pp. 1545-1554
    • Meijer, L.1    Azzi, L.2    Wang, J.Y.3
  • 26
    • 0028062756 scopus 로고
    • XMAP from Xenopus eggs promotes rapid plus end assembly of microtubules and rapid microtubule polymer turnover
    • Vasquez R. J., Gard D. L., Cassimeris L. XMAP from Xenopus eggs promotes rapid plus end assembly of microtubules and rapid microtubule polymer turnover. J. Cell. Biol. 127:1994;985-993.
    • (1994) J. Cell. Biol. , vol.127 , pp. 985-993
    • Vasquez, R.J.1    Gard, D.L.2    Cassimeris, L.3
  • 27
    • 0032101370 scopus 로고    scopus 로고
    • ZYG-9, a Caenorhabditis elegans protein required for microtubule organization and function, is a component of meiotic and mitotic spindle poles
    • Matthews L. R., Carter P., Thierry M. D., Kemphues K. ZYG-9, a Caenorhabditis elegans protein required for microtubule organization and function, is a component of meiotic and mitotic spindle poles. J. Cell. Biol. 141:1998;1159-1168.
    • (1998) J. Cell. Biol. , vol.141 , pp. 1159-1168
    • Matthews, L.R.1    Carter, P.2    Thierry, M.D.3    Kemphues, K.4
  • 28
    • 0032100813 scopus 로고    scopus 로고
    • The yeast spindle pole body component Spc72p interacts with Stu2p and is required for proper microtubule assembly
    • Chen X. P., Yin H., Huffaker T. C. The yeast spindle pole body component Spc72p interacts with Stu2p and is required for proper microtubule assembly. J. Cell. Biol. 141:1998;1169-1179.
    • (1998) J. Cell. Biol. , vol.141 , pp. 1169-1179
    • Chen, X.P.1    Yin, H.2    Huffaker, T.C.3
  • 29
    • 0028983320 scopus 로고
    • P93dis1, which is required for sister chromatid separation, is a novel microtubule and spindle pole body-associating protein phosphorylated at the Cdc2 target sites
    • Nabeshima K., Kurooka H., Takeuchi M., Kinoshita K., Nakaseko Y., Yanagida M. p93dis1, which is required for sister chromatid separation, is a novel microtubule and spindle pole body-associating protein phosphorylated at the Cdc2 target sites. Genes Dev. 9:1995;1572-1585.
    • (1995) Genes Dev. , vol.9 , pp. 1572-1585
    • Nabeshima, K.1    Kurooka, H.2    Takeuchi, M.3    Kinoshita, K.4    Nakaseko, Y.5    Yanagida, M.6
  • 30
    • 0025037989 scopus 로고
    • Regulation of microtubule dynamics by cdc2 protein kinase in cell-free extracts of Xenopus eggs
    • Verde F., Labbe J. C., Doree M., Karsenti E. Regulation of microtubule dynamics by cdc2 protein kinase in cell-free extracts of Xenopus eggs. Nature. 343:1990;233-238.
    • (1990) Nature , vol.343 , pp. 233-238
    • Verde, F.1    Labbe, J.C.2    Doree, M.3    Karsenti, E.4
  • 31
    • 0025109181 scopus 로고
    • Real-time visualization of cell cycle-dependent changes in microtubule dynamics in cytoplasmic extracts
    • Belmont L. D., Hyman A. A., Sawin K. E., Mitchison T. J. Real-time visualization of cell cycle-dependent changes in microtubule dynamics in cytoplasmic extracts. Cell. 62:1990;579-589.
    • (1990) Cell , vol.62 , pp. 579-589
    • Belmont, L.D.1    Hyman, A.A.2    Sawin, K.E.3    Mitchison, T.J.4
  • 32
    • 0011214518 scopus 로고    scopus 로고
    • Remmoval of MAP4 from microtubules in vivo produces no observable phenotype at cellular level
    • Wang X. M., Peloquin J. G., Zhai Y., Bulinski J. C., Borisy G. G. Remmoval of MAP4 from microtubules in vivo produces no observable phenotype at cellular level. J. Cell Biol. 132:1996;345-357.
    • (1996) J. Cell Biol. , vol.132 , pp. 345-357
    • Wang, X.M.1    Peloquin, J.G.2    Zhai, Y.3    Bulinski, J.C.4    Borisy, G.G.5
  • 33
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes G., Ebneth A., Preuss U., Mandelkow E. M., Mandelkow E. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell. 89:1997;297-308.
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 34
    • 0029965781 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics
    • Illenberger S., Drewes G., Trinczek B., Biernat J., Meyer H. E., Olmsted J. B., Mandelkow E. M., Mandelkow E. Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics. J. Biol. Chem. 271:1996;10834-10843.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10834-10843
    • Illenberger, S.1    Drewes, G.2    Trinczek, B.3    Biernat, J.4    Meyer, H.E.5    Olmsted, J.B.6    Mandelkow, E.M.7    Mandelkow, E.8
  • 35
    • 0027985351 scopus 로고
    • Effect on microtubule dynamics of XMAP230, a microtubule-associated protein present in Xenopus laevis eggs and dividing cells
    • Andersen S. S. L., Buendia B., Dominguez J. E., Sawyer A., Karsenti E. Effect on microtubule dynamics of XMAP230, a microtubule-associated protein present in Xenopus laevis eggs and dividing cells. J. Cell. Biol. 127:1994;1289-1299.
    • (1994) J. Cell. Biol. , vol.127 , pp. 1289-1299
    • Andersen, S.S.L.1    Buendia, B.2    Dominguez, J.E.3    Sawyer, A.4    Karsenti, E.5
  • 36
    • 0030663597 scopus 로고    scopus 로고
    • XMAP310: A Xenopus rescue-promoting factor localized to the mitotic spindle
    • Andersen S. S. L., Karsenti E. XMAP310: A Xenopus rescue-promoting factor localized to the mitotic spindle. J. Cell. Biol. 139:1997;975-983.
    • (1997) J. Cell. Biol. , vol.139 , pp. 975-983
    • Andersen, S.S.L.1    Karsenti, E.2
  • 37
    • 0026649581 scopus 로고
    • Regulation of a major microtubule-associated protein by MPF and MAp kinase
    • Shiina N., Moriguchi T., Ohta K., Gotoh Y., Nishida E. Regulation of a major microtubule-associated protein by MPF and MAp kinase. EMBO J. 11:1992;3977-3984.
    • (1992) EMBO J. , vol.11 , pp. 3977-3984
    • Shiina, N.1    Moriguchi, T.2    Ohta, K.3    Gotoh, Y.4    Nishida, E.5
  • 38
    • 0032467955 scopus 로고    scopus 로고
    • Xenopus interphase and mitotic microtubule-associated proteins differentially suppress microtubule dynamics in vitro
    • Andersen S. S. L. Xenopus interphase and mitotic microtubule-associated proteins differentially suppress microtubule dynamics in vitro. Cell Motil. Cytoskeleton. 41:1998;202-213.
    • (1998) Cell Motil. Cytoskeleton , vol.41 , pp. 202-213
    • Andersen, S.S.L.1
  • 39
    • 85029462872 scopus 로고
    • Promotion of microtubule assembly by XMAP215 is regulated by phosphorylation
    • Vasquez R. J., Gard D. L., Cassimeris L. Promotion of microtubule assembly by XMAP215 is regulated by phosphorylation. Mol. Biol. Cell. Suppl. 6. 1995;256a.
    • (1995) Mol. Biol. Cell. Suppl. 6
    • Vasquez, R.J.1    Gard, D.L.2    Cassimeris, L.3
  • 40
    • 0025193506 scopus 로고
    • Substrates for p34cdc2: In vivo veritas
    • Moreno S., Nurse P. Substrates for p34cdc2: In vivo veritas. Cell. 61:1990;549-551.
    • (1990) Cell , vol.61 , pp. 549-551
    • Moreno, S.1    Nurse, P.2
  • 41
    • 0029786994 scopus 로고    scopus 로고
    • Cytoplasmic localization of mitogen-activated protein kinase kinase directed by its NH2-terminal leucine-rich short amino acid sequence which acts as a nuclear export signal
    • Fukuda M., Gotoh I., Gotoh Y. Cytoplasmic localization of mitogen-activated protein kinase kinase directed by its NH2-terminal leucine-rich short amino acid sequence which acts as a nuclear export signal. J. Biol. Chem. 271:1996;20024-20028.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20024-20028
    • Fukuda, M.1    Gotoh, I.2    Gotoh, Y.3
  • 42
    • 0032525308 scopus 로고    scopus 로고
    • Nuclear export of cyclin B1 and its possible role in the DNA damage-induced G2 checkpoint
    • Toyoshima F., Moriguchi T., Wada A., Fukuda M., Nishida E. Nuclear export of cyclin B1 and its possible role in the DNA damage-induced G2 checkpoint. EMBO J. 17:1998;2728-2735.
    • (1998) EMBO J. , vol.17 , pp. 2728-2735
    • Toyoshima, F.1    Moriguchi, T.2    Wada, A.3    Fukuda, M.4    Nishida, E.5
  • 43
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from nucleus
    • Wen W., Meinkoth J. L., Tsien R. Y., Taylor S. S. Identification of a signal for rapid export of proteins from nucleus. Cell. 82:1995;463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 44
    • 0032528001 scopus 로고    scopus 로고
    • Control of cyclin B1 localization through regulated binding of the nuclear export factor
    • Yang J., Bardes E. S., Moore J. D., Brennan J., Powers M. A., Kornbluth S. Control of cyclin B1 localization through regulated binding of the nuclear export factor. Genes Dev. 12:1998;2131-2143.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.