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Volumn 12, Issue 14, 1998, Pages 2131-2143

Control of Cyclin B1 localization through regulated binding of the nuclear export factor CRM1

Author keywords

Cell cycle; Cellular localization; CRM1; CRS phosphorylation; Cyclin B1; Nuclear export

Indexed keywords

CELL ANTIGEN; CYCLIN B1; CYCLIN DEPENDENT KINASE; LEPTOMYCIN B; RECEPTOR; UNCLASSIFIED DRUG;

EID: 0032528001     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.12.14.2131     Document Type: Article
Times cited : (285)

References (53)
  • 2
    • 0029894726 scopus 로고    scopus 로고
    • Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay
    • Bogerd, H.P., R.A. Fridell, R.E. Benson, J. Hua, and B.R. Cullen. 1996. Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay. Mol. Cell. Biol. 16: 4207-4214.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4207-4214
    • Bogerd, H.P.1    Fridell, R.A.2    Benson, R.E.3    Hua, J.4    Cullen, B.R.5
  • 3
    • 0030793194 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport of macromolecules
    • Corbett, A.H. and P.A. Silver. 1997. Nucleocytoplasmic transport of macromolecules. Microbiol. Mol. Biol. Rev. 61: 193-211.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 193-211
    • Corbett, A.H.1    Silver, P.A.2
  • 4
    • 0031005268 scopus 로고    scopus 로고
    • From nucleoporins to nuclear pore complexes
    • Doye, V. and E. Hurt. 1997. From nucleoporins to nuclear pore complexes. Curr. Opin. Cell Biol. 9: 401-411.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 401-411
    • Doye, V.1    Hurt, E.2
  • 5
    • 0025938467 scopus 로고
    • The cdc25 protein contains an intinsic phosphatase activity
    • Dunphy, W.G. and A. Kumagai. 1991. The cdc25 protein contains an intinsic phosphatase activity. Cell 67: 189-196.
    • (1991) Cell , vol.67 , pp. 189-196
    • Dunphy, W.G.1    Kumagai, A.2
  • 6
    • 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., J. Huber, W.C. Boelens, I.W. Mattaj, and R. Lührmann. 1995. 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) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Lührmann, R.5
  • 7
    • 0030924190 scopus 로고    scopus 로고
    • Crm1 is an export receptor for Leucine-rich nuclear export signals
    • Fornerod, M., M. Ohno, M. Yoshida, and I.W. Mattaj. 1997. Crm1 is an export receptor for Leucine-rich nuclear export signals. Cell 90: 1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 8
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda, M., S. Asano, T. Nakamura, M. Adachi, M. Yoshida, M. Yanagida, and E. Nishida. 1997. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390: 308-311.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 9
    • 0026011212 scopus 로고
    • Cyclin B in Xenopus oocytes: Implications for the mechanism of pre-MPF activation
    • Gautier, J. and J.L. Maller. 1991. Cyclin B in Xenopus oocytes: Implications for the mechanism of pre-MPF activation. EMBO J. 10: 177-182.
    • (1991) EMBO J. , vol.10 , pp. 177-182
    • Gautier, J.1    Maller, J.L.2
  • 10
    • 0025936510 scopus 로고
    • Cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2
    • Gautier, J., M.J. Solomon, R.N. Booher, J.F. Bazan, and M.W. Kirschner. 1991. Cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2. Cell 67: 197.
    • (1991) Cell , vol.67 , pp. 197
    • Gautier, J.1    Solomon, M.J.2    Booher, R.N.3    Bazan, J.F.4    Kirschner, M.W.5
  • 11
    • 0026709066 scopus 로고
    • Cdc25 is a nuclear protein expressed constitutively throughout the cell cycle in nontransformed mammalian cells
    • Girard, F., U. Strausfeld, J.C. Cavadore, P. Russell, A. Fernandez, and N.J. Lamb. 1992. Cdc25 is a nuclear protein expressed constitutively throughout the cell cycle in nontransformed mammalian cells. J. Cell Biol. 118: 785-794.
    • (1992) J. Cell Biol. , vol.118 , pp. 785-794
    • Girard, F.1    Strausfeld, U.2    Cavadore, J.C.3    Russell, P.4    Fernandez, A.5    Lamb, N.J.6
  • 13
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Gorlich, D. and I.W. Mattaj. 1996. Nucleocytoplasmic transport. Science 271: 1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Gorlich, D.1    Mattaj, I.W.2
  • 14
    • 0029059548 scopus 로고
    • Distinct functions for the two importin subunits in nuclear protein import
    • Gorlich, D., F. Vogel, A.D. Mills, E. Hartmann, and R.A. Laskey. 1995. Distinct functions for the two importin subunits in nuclear protein import. Nature 377: 246-248.
    • (1995) Nature , vol.377 , pp. 246-248
    • Gorlich, D.1    Vogel, F.2    Mills, A.D.3    Hartmann, E.4    Laskey, R.A.5
  • 15
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • Gorlich, D., S. Prehn, R.A. Laskey, and E. Hartmann. 1994. Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79: 767-778.
    • (1994) Cell , vol.79 , pp. 767-778
    • Gorlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 16
    • 0027244234 scopus 로고
    • Human weel maintains mitotic timing by protecting the nucleus from cytoplasmically activated cdc2 kinase
    • Heald, R., M. McLoughlin, and F. McKeon. 1993. Human weel maintains mitotic timing by protecting the nucleus from cytoplasmically activated cdc2 kinase. Cell 74: 463-474.
    • (1993) Cell , vol.74 , pp. 463-474
    • Heald, R.1    McLoughlin, M.2    McKeon, F.3
  • 17
    • 0025800585 scopus 로고
    • Phosphorylation of Xenopus cyclins B1 and B2 is not required for cell cycle transitions
    • Izumi, T. and J.L. Maller. 1991. Phosphorylation of Xenopus cyclins B1 and B2 is not required for cell cycle transitions. Mol. Cell. Biol. 11: 3860-3867.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3860-3867
    • Izumi, T.1    Maller, J.L.2
  • 18
    • 0027075988 scopus 로고
    • Periodic changes in phosphorylation of the Xenopus cdc25 phosphatase regulate its activity
    • Izumi, T., D.H. Walker, and I.L. Maller. 1992. Periodic changes in phosphorylation of the Xenopus cdc25 phosphatase regulate its activity. Mol. Biol. Cell 3: 927-939.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 927-939
    • Izumi, T.1    Walker, D.H.2    Maller, I.L.3
  • 19
    • 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., M. Firth, and J. Pines. 1995. 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) EMBO J. , vol.14 , pp. 1646-1654
    • Jackman, M.1    Firth, M.2    Pines, J.3
  • 20
    • 0025874692 scopus 로고
    • On the synthesis and destruction of A- and B-type cyclins during oogenesis and miotic maturation in Xenopus laevis
    • Kobayashi, H., J. Minshull, C. Ford, R. Golsteyn, R. Poon, and T. Hunt. 1991. On the synthesis and destruction of A-and B-type cyclins during oogenesis and miotic maturation in Xenopus laevis. J. Cell. Biol. 114: 755-765.
    • (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
  • 22
    • 0026689359 scopus 로고
    • cdc2 phosphorylation site mutants: Effects upon cell cycle progression in the fission yeast Schizosaccharomyes pombe
    • cdc2 phosphorylation site mutants: Effects upon cell cycle progression in the fission yeast Schizosaccharomyes pombe. J. Cell Sci. 102: 43-53.
    • (1992) J. Cell Sci. , vol.102 , pp. 43-53
    • Krek, W.1    Marks, J.2    Schmitz, N.3    Nigg, E.A.4    Simanis, V.5
  • 23
    • 0342276108 scopus 로고    scopus 로고
    • Export of Importin α from the nucleus is mediated by a specific nuclear transport factor
    • Kutay, U.B., F.R. Bischoff, S. Kostka, R. Kraft, and D. Gorlich. 1997. Export of Importin α from the nucleus is mediated by a specific nuclear transport factor. Cell 90: 1061-1071.
    • (1997) Cell , vol.90 , pp. 1061-1071
    • Kutay, U.B.1    Bischoff, F.R.2    Kostka, S.3    Kraft, R.4    Gorlich, D.5
  • 24
    • 0029145653 scopus 로고
    • Requirement for phosphorylation of cyclin B1 for Xenopus oocyte maturtion
    • Li, J., A.N. Meyer, and D.J. Donoghue. 1995. Requirement for phosphorylation of cyclin B1 for Xenopus oocyte maturtion. Mol. Biol. Cell 6: 1111-1124.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1111-1124
    • Li, J.1    Meyer, A.N.2    Donoghue, D.J.3
  • 25
    • 0031028382 scopus 로고    scopus 로고
    • Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation
    • _. 1997. Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation. Proc. Natl. Acad. Sci. 94: 502-507.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 502-507
  • 26
    • 0031053117 scopus 로고    scopus 로고
    • The human Myt1 kinase preferentially phosphorylates cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi
    • Lu, F., J.J. Stanton, Z. Wu, and H. Piwnica-Worms. 1997. The human Myt1 kinase preferentially phosphorylates cdc2 on threonine 14 and localizes to the endoplasmic reticulum and Golgi. Mol. Cell. Biol. 17: 571-583.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 571-583
    • Lu, F.1    Stanton, J.J.2    Wu, Z.3    Piwnica-Worms, H.4
  • 27
    • 0025335266 scopus 로고
    • Non-aqueous isolation of transcriptionally active nuclei from Xenopus oocytes
    • Lund, E. and P.L. Paine. 1990. Non-aqueous isolation of transcriptionally active nuclei from Xenopus oocytes. Meth. Enzymol. 181: 36-43.
    • (1990) Meth. Enzymol. , vol.181 , pp. 36-43
    • Lund, E.1    Paine, P.L.2
  • 28
    • 0029000155 scopus 로고
    • Cell cycle regulation of human WEEl
    • McGowan, C.H. and P. Russell. 1995. Cell cycle regulation of human WEEl. EMBO J. 14: 2166-2175.
    • (1995) EMBO J. , vol.14 , pp. 2166-2175
    • McGowan, C.H.1    Russell, P.2
  • 29
    • 0024470772 scopus 로고
    • Cyclin is a component of the sea urchin M-phase specific histone H1 kinase
    • Meijer, L., D. Arion, R. Golsteyn, J. Pines, L. Brizuela, T. Hunt, and D. Beach. 1989. Cyclin is a component of the sea urchin M-phase specific histone H1 kinase. EMBO J. 8: 2275-2282.
    • (1989) EMBO J. , vol.8 , pp. 2275-2282
    • Meijer, L.1    Arion, D.2    Golsteyn, R.3    Pines, J.4    Brizuela, L.5    Hunt, T.6    Beach, D.7
  • 30
    • 0029871772 scopus 로고    scopus 로고
    • Nuclear transport of human immunodeficiency virus type 1, visna virus, and equine infectious anemia Rev proteins: Identification of a family of transferrable export signals
    • Meyer, B.E., J.L. Meinkoth, and M.H. Malim. 1996. Nuclear transport of human immunodeficiency virus type 1, visna virus, and equine infectious anemia Rev proteins: Identification of a family of transferrable export signals. J. Virol. 70: 2350-2359.
    • (1996) J. Virol. , vol.70 , pp. 2350-2359
    • Meyer, B.E.1    Meinkoth, J.L.2    Malim, M.H.3
  • 31
    • 0026569665 scopus 로고
    • The cdc25 M-Phase inducer: An unconventional protein phosphatase
    • Millar, J.B.A. and P. Russell. 1992. The cdc25 M-Phase inducer: An unconventional protein phosphatase. Cell 68: 407-410.
    • (1992) Cell , vol.68 , pp. 407-410
    • Millar, J.B.A.1    Russell, P.2
  • 33
    • 0028998865 scopus 로고
    • Cell cycle regulation of a Xenopus Weel-like kinase
    • Mueller, P.R., T.R. Coleman, and W.G. Dunphy. 1995a. Cell cycle regulation of a Xenopus Weel-like kinase. Mol. Biol. Cell 6: 119-134.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 119-134
    • Mueller, P.R.1    Coleman, T.R.2    Dunphy, W.G.3
  • 34
    • 0028783413 scopus 로고
    • Myt1: A membrane-associated inhibitory kinase that phosphorylates cdc2 on both Threonine-14 and Tyrosine-15
    • Mueller, P.R., T.R. Coleman, A. Kumagai, and W.G. Dunphy. 1995b. Myt1: 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    Kumagai, A.3    Dunphy, W.G.4
  • 35
    • 0026703325 scopus 로고
    • Creative blocks: Cell-cycle checkpoints and feedback controls
    • Murray, AW. 1992. Creative blocks: Cell-cycle checkpoints and feedback controls. Nature 359: 599-604.
    • (1992) Nature , vol.359 , pp. 599-604
    • Murray, A.W.1
  • 36
    • 0031260540 scopus 로고    scopus 로고
    • The importin-beta family member Crmlp bridges the interaction between Rev and the nuclear pore complex during nuclear export
    • Neville, M.S., F. Stutz, L. Lee, L.I. Davis, and M. Rosbash. 1997. The importin-beta family member Crmlp bridges the interaction between Rev and the nuclear pore complex during nuclear export. Curr. Biol. 7: 767-775.
    • (1997) Curr. Biol. , vol.7 , pp. 767-775
    • Neville, M.S.1    Stutz, F.2    Lee, L.3    Davis, L.I.4    Rosbash, M.5
  • 37
    • 0025988705 scopus 로고
    • Regulatory phosphorylation of the p34cdc2 protein kinase in vertebrates
    • Norbury, C., J. Blow, and P. Nurse. 1991. Regulatory phosphorylation of the p34cdc2 protein kinase in vertebrates. EMBO J. 10: 3321-3329.
    • (1991) EMBO J. , vol.10 , pp. 3321-3329
    • Norbury, C.1    Blow, J.2    Nurse, P.3
  • 38
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of Crm1 in signal-mediated nuclear protein export
    • Ossareh-Nazari, B., F. Bachelerie, and C. Dargemont. 1997. Evidence for a role of Crm1 in signal-mediated nuclear protein export. Science 278: 141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 39
    • 0026014878 scopus 로고
    • Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport
    • Pines, J. and T. Hunter. 1991. 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) J. Cell Biol. , vol.115 , pp. 1-17
    • Pines, J.1    Hunter, T.2
  • 40
    • 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 T. Hunter. 1994. 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) EMBO J. , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 42
    • 0028950991 scopus 로고
    • Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins
    • Radu, A., G. Blobel, and M.S. Moore. 1995. Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Proc. Natl. Acad. Sci. 92: 1769-1773.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 1769-1773
    • Radu, A.1    Blobel, G.2    Moore, M.S.3
  • 43
    • 0030879014 scopus 로고    scopus 로고
    • Requirement for guanosine triphosphate-bound Ran for signal-mediated nuclear protein export
    • Richards, S.A., K.L. Carey, and I.G. Macara. 1997. Requirement for guanosine triphosphate-bound Ran for signal-mediated nuclear protein export. Science 276: 1842-1844.
    • (1997) Science , vol.276 , pp. 1842-1844
    • Richards, S.A.1    Carey, K.L.2    Macara, I.G.3
  • 44
    • 0029911757 scopus 로고    scopus 로고
    • The human Cas protein which is homologous to CSE1 yeast chromosome segregation gene product is associated with microtubules and mitotic spindle
    • Scherf, R., I. Pastan, N.C. Willingham, and U. Brinkmann. 1996. The human Cas protein which is homologous to CSE1 yeast chromosome segregation gene product is associated with microtubules and mitotic spindle. Proc. Natl. Acad. Sci. 93: 2670-2674.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 2670-2674
    • Scherf, R.1    Pastan, I.2    Willingham, N.C.3    Brinkmann, U.4
  • 45
    • 0027058705 scopus 로고
    • Chromosome condensation caused by loss of RCC1 function requires the cdc25C protein that is located in the cytoplasm
    • Seki, T., K. Yamashita, H. Nishitani, T. Takagi, P. Russell, and T. Nishimoto. 1992. Chromosome condensation caused by loss of RCC1 function requires the cdc25C protein that is located in the cytoplasm. Mol. Biol. Cell 3: 1373-1388.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1373-1388
    • Seki, T.1    Yamashita, K.2    Nishitani, H.3    Takagi, T.4    Russell, P.5    Nishimoto, T.6
  • 47
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade, K., C.S. Ford, C. Guthrie, and K. Weiss. 1997. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90: 1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weiss, K.4
  • 49
    • 0024560509 scopus 로고
    • Formation of gap junctions by expression of connexins in Xenopus oocyte pairs
    • Swenson, K.I., J.R. Jordan, E.C. Beyer, and D.L. Paul. 1989. Formation of gap junctions by expression of connexins in Xenopus oocyte pairs. Cell 57: 145-155.
    • (1989) Cell , vol.57 , pp. 145-155
    • Swenson, K.I.1    Jordan, J.R.2    Beyer, E.C.3    Paul, D.L.4
  • 50
    • 0030886673 scopus 로고    scopus 로고
    • Nuclear export receptors: From Importin to Exportin
    • Ullman, K.S., M.A. Powers, and D.J. Forbes. 1997. Nuclear export receptors: From Importin to Exportin. Cell 90: 967-970.
    • (1997) Cell , vol.90 , pp. 967-970
    • Ullman, K.S.1    Powers, M.A.2    Forbes, D.J.3
  • 51
    • 0029048491 scopus 로고
    • Regulation of the human Wee1Hu CDK tyrosine-15 kinase during the cell cycle
    • Watanabe, N., M. Broome, and T. Hunter. 1994. Regulation of the human Wee1Hu CDK tyrosine-15 kinase during the cell cycle. EMBO J. 14: 1878-1891.
    • (1994) EMBO J. , vol.14 , pp. 1878-1891
    • Watanabe, N.1    Broome, M.2    Hunter, T.3
  • 52
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., J.L. Meinkoth, R.Y. Tsien, and S.S. Taylor. 1995. Identification of a signal for rapid export of proteins from the nucleus. Cell 82: 463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 53
    • 0029955482 scopus 로고    scopus 로고
    • Spatial organization of the Nim1-wee1-cdc2 mitotic control network in Schizosaccharomyces pombe
    • Wu, L., K. Shiozaki, H. Aligue, and P. Russell. 1996. Spatial organization of the Nim1-wee1-cdc2 mitotic control network in Schizosaccharomyces pombe. Mol. Biol. Cell 7: 1749-1758.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1749-1758
    • Wu, L.1    Shiozaki, K.2    Aligue, H.3    Russell, P.4


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