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Volumn 138, Issue 5, 1997, Pages 1105-1116

A dual-specificity phosphatase Cdc25B is an unstable protein and triggers p34(cdc2)/cyclin B activation in hamster BHK21 cells arrested with hydroxyurea

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN B; CYCLIN DEPENDENT KINASE; HISTONE H1; HYDROXYUREA; PHOSPHOTRANSFERASE;

EID: 0030884275     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.138.5.1105     Document Type: Article
Times cited : (84)

References (64)
  • 2
    • 0026419320 scopus 로고
    • Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1
    • Bischoff, F.R., and H. Ponstingle. 1991. Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature (Lond.). 354:80-82.
    • (1991) Nature (Lond.) , vol.354 , pp. 80-82
    • Bischoff, F.R.1    Ponstingle, H.2
  • 3
    • 0024294414 scopus 로고
    • Regulation of MPF activity in vitro
    • Cyert, M.S., and M.W. Kirschner. 1988. Regulation of MPF activity in vitro. Cell 53:185-195.
    • (1988) Cell , vol.53 , pp. 185-195
    • Cyert, M.S.1    Kirschner, M.W.2
  • 4
    • 0029975651 scopus 로고    scopus 로고
    • The thermolability of nuclear protein import in tsBN2 cells is suppressed by microinjected Ran-GTP or Ran-GDP, but not by RanQ69L or RanT24N
    • Dickmanns, A., F.R. Bischoff, C. Marshallsay, R. Luhrmann, H. Ponstingle, and E. Fanning. 1996. The thermolability of nuclear protein import in tsBN2 cells is suppressed by microinjected Ran-GTP or Ran-GDP, but not by RanQ69L or RanT24N. J. Cell Science. 109:1449-1457.
    • (1996) J. Cell Science , vol.109 , pp. 1449-1457
    • Dickmanns, A.1    Bischoff, F.R.2    Marshallsay, C.3    Luhrmann, R.4    Ponstingle, H.5    Fanning, E.6
  • 6
    • 0028332528 scopus 로고
    • The decision to enter mitosis
    • Dunphy, W.G. 1994. The decision to enter mitosis. Trends Cell Biol. 4:202-207.
    • (1994) Trends Cell Biol. , vol.4 , pp. 202-207
    • Dunphy, W.G.1
  • 7
    • 0020961333 scopus 로고
    • Cyclin: A protein specified by maternal mRNA in Sea Urchin eggs that is destroyed at each cleavage division
    • Evans, T., E.T. Rosenthal, J. Youngblom, D. Distel, and T. Hunt. 1983. Cyclin: a protein specified by maternal mRNA in Sea Urchin eggs that is destroyed at each cleavage division. Cell. 33:389-396.
    • (1983) Cell , vol.33 , pp. 389-396
    • Evans, T.1    Rosenthal, E.T.2    Youngblom, J.3    Distel, D.4    Hunt, T.5
  • 8
    • 0027296041 scopus 로고
    • The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr 161 and its homologues
    • Fesquet, D., J.C. Labbe, J. Derancourt, J.P. Capony, S. Galas, F. Girard, T. Lorca, J. Shuttle-worth, M. Doree, and J.C. Cavadore. 1993. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr 161 and its homologues. EMBO (Eur. Mol. Biol. Organ.) J. 12:3111-3121.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 3111-3121
    • Fesquet, D.1    Labbe, J.C.2    Derancourt, J.3    Capony, J.P.4    Galas, S.5    Girard, F.6    Lorca, T.7    Shuttle-worth, J.8    Doree, M.9    Cavadore, J.C.10
  • 9
    • 0025924328 scopus 로고
    • Fission yeast p107wee1 mitotic inhibitor is a tyrosine/serine kinase
    • Featherstone, C., and P. Russell. 1991. Fission yeast p107wee1 mitotic inhibitor is a tyrosine/serine kinase. Nature (Lond.). 349:808-811.
    • (1991) Nature (Lond.) , vol.349 , pp. 808-811
    • Featherstone, C.1    Russell, P.2
  • 10
    • 0025856292 scopus 로고
    • The maternally expressed Drosophila gene encoding the chromatin-binding protein BJ1 is a homolog of the vertebrate gene Regulator of Chromatin Condensation, RCC1
    • Frasch, M. 1991. The maternally expressed Drosophila gene encoding the chromatin-binding protein BJ1 is a homolog of the vertebrate gene Regulator of Chromatin Condensation, RCC1. EMBO (Eur. Mol. Biol. Organ.) J. 10: 1225-1236.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 1225-1236
    • Frasch, M.1
  • 12
    • 0026319225 scopus 로고
    • Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: Evidence for multiple roles of mitotic cyclins
    • Galaktionov, K., and D. Beach. 1991. Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins. Cell. 67:1181-1194.
    • (1991) Cell , vol.67 , pp. 1181-1194
    • Galaktionov, K.1    Beach, D.2
  • 14
    • 0027244234 scopus 로고
    • Human wee1 maintains mitotic timing by protecting the nucleus from cytoplasmically activated cdc2 kinase
    • Heald, R., M. McLoughlin, and F. McKeon. 1993. Human wee1 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
  • 15
    • 0020804563 scopus 로고
    • Ubiquitin; roles in protein modification and breakdown
    • Hershko, A. 1983. Ubiquitin; roles in protein modification and breakdown. Cell. 34:11-12.
    • (1983) Cell , vol.34 , pp. 11-12
    • Hershko, A.1
  • 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., P.R. Clarke, M.J. Marcote, E. Karsenti, and G. Draetta. 1993. Phosphorylation and activation of human cdc25-C by cdc2/cyclin B and its involvement in the self-amplification of MPF at mitosis. EMBO (Eur. Mol. Biol. Organ.) J. 12:53-63.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 53-63
    • Hoffmann, I.1    Clarke, P.R.2    Marcote, M.J.3    Karsenti, E.4    Draetta, G.5
  • 18
    • 0027339731 scopus 로고
    • Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase
    • Honda, R., Y. Ohba, A. Nagata, H. Okayama, and H. Yasuda. 1993. Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase. FEBS (Fed. Eur. Biochem. Soc.) Lett. 318:331-334.
    • (1993) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.318 , pp. 331-334
    • Honda, R.1    Ohba, Y.2    Nagata, A.3    Okayama, H.4    Yasuda, H.5
  • 19
    • 0027746003 scopus 로고
    • Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase
    • Izumi, T., and J.L. Maller. 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
  • 20
    • 0027075988 scopus 로고
    • Periodic changes in phosphorylation of the Xenopus cdc25 phosphatase regulate its activity
    • Izumi, T., D.H. Walker, and J.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, J.L.3
  • 22
    • 0026719599 scopus 로고
    • Regulation of the cdc25 protein during the cell cycle in Xenopus extracts
    • Kumagai, A., and W.G. Dunphy. 1992. Regulation of the cdc25 protein during the cell cycle in Xenopus extracts. Cell. 70:139-151.
    • (1992) Cell , vol.70 , pp. 139-151
    • Kumagai, A.1    Dunphy, W.G.2
  • 23
  • 24
    • 0029821131 scopus 로고    scopus 로고
    • Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts
    • Kumagai, A., and W.G. Dunphy. 1996. Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts. Science (Wash. DC). 273:1377-1380.
    • (1996) Science (Wash. DC) , vol.273 , pp. 1377-1380
    • Kumagai, A.1    Dunphy, W.G.2
  • 26
    • 0026018749 scopus 로고
    • INH, a negative regulator of MPF, is a form of protein phosphatase 2A
    • Lee, T.H., M.J. Solomon, M.C. Mumby, and M.W. Kirschner. 1991. INH, a negative regulator of MPF, is a form of protein phosphatase 2A. Cell. 64:415-423.
    • (1991) Cell , vol.64 , pp. 415-423
    • Lee, T.H.1    Solomon, M.J.2    Mumby, M.C.3    Kirschner, M.W.4
  • 27
    • 0028348011 scopus 로고
    • Inhibition of cdc2 activation by INH/PP2A
    • Lee, T.H., C. Turck, and M.W. Kirschner. 1994a. Inhibition of cdc2 activation by INH/PP2A. Mol. Biol. Cell. 5:323-338.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 323-338
    • Lee, T.H.1    Turck, C.2    Kirschner, M.W.3
  • 31
    • 0027714921 scopus 로고
    • Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor
    • Melchior, F., B. Paschal, E. Evans, and L. Gerace. 1993. Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor. J. Cell Biol. 123: 1649-1659.
    • (1993) J. Cell Biol. , vol.123 , pp. 1649-1659
    • Melchior, F.1    Paschal, B.2    Evans, E.3    Gerace, L.4
  • 33
    • 0025827294 scopus 로고
    • Xenopus oocyte maturation does not require new cyclin synthesis
    • Minshull, J., A. Murray, A. Colman, and T. Hunt. 1991. Xenopus oocyte maturation does not require new cyclin synthesis. J. Cell Biol. 114:767-772.
    • (1991) J. Cell Biol. , vol.114 , pp. 767-772
    • Minshull, J.1    Murray, A.2    Colman, A.3    Hunt, T.4
  • 34
    • 0022971281 scopus 로고
    • Protein tyrosine phosphorylation in the cell cycle of GALB/c 3T3 fibroblasts
    • Morla, A., and J.Y.J. Wang. 1986. Protein tyrosine phosphorylation in the cell cycle of GALB/c 3T3 fibroblasts. Proc. Natl. Acad. Sci. USA. 83:8191-8195.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8191-8195
    • Morla, A.1    Wang, J.Y.J.2
  • 35
    • 0027376308 scopus 로고
    • The GTP-binding protein Ran/TC4 is required for protein import into the nucleus
    • Moore, M.S., and G. Blobel. 1993. The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature (Lond.). 365:661-663.
    • (1993) Nature (Lond.) , vol.365 , pp. 661-663
    • Moore, M.S.1    Blobel, G.2
  • 36
    • 0028998865 scopus 로고
    • Cell cycle regulation of a Xenopus wee1-like kinase
    • Mueller, P.R., T.R. Coleman, and W.G. Dunphy. 1995a. Cell cycle regulation of a Xenopus wee1-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
  • 37
    • 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 (Wash. DC). 270:86-90.
    • (1995) Science (Wash. DC) , vol.270 , pp. 86-90
    • Mueller, P.R.1    Coleman, T.R.2    Kumagai, A.3    Dunphy, W.G.4
  • 39
    • 0030006130 scopus 로고    scopus 로고
    • Pub1 acts as an E6-AP-like protein ubiquitin ligase in the degradation of cdc25
    • Nefsky, B., and D. Beach. 1996. Pub1 acts as an E6-AP-like protein ubiquitin ligase in the degradation of cdc25. EMBO (Eur. Mol. Biol. Organ.) J. 15: 1301-1312.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 1301-1312
    • Nefsky, B.1    Beach, D.2
  • 41
    • 0019867487 scopus 로고
    • The synthesis of protein(s) for chromosome condensation may be regulated by a post-transcriptional mechanism
    • Nishimoto, T., R. Ishida, K. Ajiro, S. Yamamoto, and T. Takahashi. 1981. The synthesis of protein(s) for chromosome condensation may be regulated by a post-transcriptional mechanism. J. Cell. Physiol. 109:299-308.
    • (1981) J. Cell. Physiol. , vol.109 , pp. 299-308
    • Nishimoto, T.1    Ishida, R.2    Ajiro, K.3    Yamamoto, S.4    Takahashi, T.5
  • 43
    • 0030934412 scopus 로고    scopus 로고
    • Yrb2p, Nup2p-related yeast protein has functional overlap with Rna1p, yeast RanGAP protein
    • Noguchi, E., N. Hayashi, N. Nakashima, and T. Nishimoto. 1997. Yrb2p, Nup2p-related yeast protein has functional overlap with Rna1p, yeast RanGAP protein. Mol. Cell. Biol. 17:2235-2246.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2235-2246
    • Noguchi, E.1    Hayashi, N.2    Nakashima, N.3    Nishimoto, T.4
  • 44
    • 0026693966 scopus 로고
    • Animal cell cycles and their control
    • Norbury, C., and P. Nurse. 1992. Animal cell cycles and their control. Annu. Rev. Biochem. 61:441-470.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 441-470
    • Norbury, C.1    Nurse, P.2
  • 45
    • 0029929097 scopus 로고    scopus 로고
    • Premature chromatin condensation induced by loss of RCC1 is inhibited by GTP- and GTPgS-Ran, but not GDP-Ran
    • Ohba, T., T. Seki, Y. Azuma, and T. Nishimoto. 1996. Premature chromatin condensation induced by loss of RCC1 is inhibited by GTP- and GTPgS-Ran, but not GDP-Ran. J. Biol. Chem. 27:14665-14667.
    • (1996) J. Biol. Chem. , vol.27 , pp. 14665-14667
    • Ohba, T.1    Seki, T.2    Azuma, Y.3    Nishimoto, T.4
  • 46
    • 0026616796 scopus 로고
    • cdc2-cyclin B complex by the human WEE1 tyrosine kinase
    • cdc2-cyclin B complex by the human WEE1 tyrosine kinase. Science (Wash. DC) 257: 1955-1957.
    • (1992) Science (Wash. DC) , vol.257 , pp. 1955-1957
    • Parker, L.L.1    Piwnica-Worms, H.2
  • 47
    • 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
  • 48
    • 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 (Eur. Mol. Biol. Organ.) J. 13:3772-3781.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 51
    • 0024280269 scopus 로고
    • Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes
    • Sagata, N., M. Oskarsson, T. Copeland, J. Brumbaugh, and G.F. Vande Woud. 1988. Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes. Nature (Lond.). 335:519-525.
    • (1988) Nature (Lond.) , vol.335 , pp. 519-525
    • Sagata, N.1    Oskarsson, M.2    Copeland, T.3    Brumbaugh, J.4    Vande Woud, G.F.5
  • 52
    • 0030046910 scopus 로고    scopus 로고
    • The search for the primary function of the Ran GTPase continues
    • Sazer, S. 1996. The search for the primary function of the Ran GTPase continues. Trends Cell Biol. 6:81-85.
    • (1996) Trends Cell Biol. , vol.6 , pp. 81-85
    • Sazer, S.1
  • 53
    • 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
  • 55
    • 0022517046 scopus 로고
    • Caffeine-induced uncoupling of mitosis from the completion of DNA replication in mammalian cells
    • Schlegel, R., and A.B. Pardee. 1986. Caffeine-induced uncoupling of mitosis from the completion of DNA replication in mammalian cells. Science (Wash. DC). 232:1264-1266.
    • (1986) Science (Wash. DC) , vol.232 , pp. 1264-1266
    • Schlegel, R.1    Pardee, A.B.2
  • 56
    • 0025035855 scopus 로고
    • MO15, a cdc2-related protein kinase involved in negative regulation of meiotic maturation of Xenopus oocytes
    • MO15, a cdc2-related protein kinase involved in negative regulation of meiotic maturation of Xenopus oocytes. EMBO (Eur. Mol. Biol. Organ.) J. 9:3233-3240.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 3233-3240
    • Shuttleworth, J.1    Godfrey, R.2    Colman, A.3
  • 60
    • 0028102739 scopus 로고
    • Loss of RCC1 leads to suppression of nuclear protein import in living cells
    • Tachibana, T., N. Imamoto, H. Seino, T. Nishimoto, and Y. Yoneda. 1994. Loss of RCC1 leads to suppression of nuclear protein import in living cells. J. Biol. Chem. 269:24542-24545.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24542-24545
    • Tachibana, T.1    Imamoto, N.2    Seino, H.3    Nishimoto, T.4    Yoneda, Y.5
  • 61
    • 0016591882 scopus 로고
    • Effects of cycloheximide on a cytoplasmic factor initiating meiotic maturation in Xenopus laevis oocytes
    • Wasserman, W.J., and Y. Masui. 1975. Effects of cycloheximide on a cytoplasmic factor initiating meiotic maturation in Xenopus laevis oocytes. Exp. Cell Res. 91:381-388.
    • (1975) Exp. Cell Res. , vol.91 , pp. 381-388
    • Wasserman, W.J.1    Masui, Y.2
  • 62
    • 0029955482 scopus 로고    scopus 로고
    • Spatial organization of the Nim1-Wee1-Cdc2 mitotic control network in Schizosaccharomyces pombe
    • Wu, L., K. Shiozaki, R. 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, R.3    Russell, P.4
  • 63
    • 0027201553 scopus 로고
    • Nim1 kinase promotes mitosis by inactivating Wee1 tyrosine kinase
    • Wu, L., and P. Russell. 1993. Nim1 kinase promotes mitosis by inactivating Wee1 tyrosine kinase. Nature (Lond.). 363:738-741.
    • (1993) Nature (Lond.) , vol.363 , pp. 738-741
    • Wu, L.1    Russell, P.2
  • 64
    • 0026580143 scopus 로고
    • Meiotic initiation by the mos protein in Xenopus
    • Yew, N., M.L. Mellini, and G.F. Vande Woude. 1992. Meiotic initiation by the mos protein in Xenopus. Nature (Lond.). 355:649-652.
    • (1992) Nature (Lond.) , vol.355 , pp. 649-652
    • Yew, N.1    Mellini, M.L.2    Vande Woude, G.F.3


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