메뉴 건너뛰기




Volumn 17, Issue 5, 1998, Pages 1315-1327

The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1

Author keywords

Cdc25; Mitosis; Peptidyl prolyl isomerase; Pin1; Plx1

Indexed keywords

CYCLIN B; CYCLOPHILIN; ISOMERASE; PROTEIN KINASE;

EID: 0032473350     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.5.1315     Document Type: Article
Times cited : (171)

References (50)
  • 3
    • 0025284348 scopus 로고
    • Completion of DNA replication is monitored by a feedback system that controls the initiation of mitosis in vitro: Studies in Xenopus
    • Dasso, M. and Newport, J.W. (1990) Completion of DNA replication is monitored by a feedback system that controls the initiation of mitosis in vitro: studies in Xenopus. Cell, 61, 811-823.
    • (1990) Cell , vol.61 , pp. 811-823
    • Dasso, M.1    Newport, J.W.2
  • 5
    • 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
  • 6
    • 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
  • 7
    • 0030768948 scopus 로고    scopus 로고
    • Cdc25 mitotic inducer targeted by Chk1 DNA damage checkpoint kinase
    • Furnari, B., Rhind, N. and Russell, P. (1997) Cdc25 mitotic inducer targeted by Chk1 DNA damage checkpoint kinase. Science, 277, 1495-1497.
    • (1997) Science , vol.277 , pp. 1495-1497
    • Furnari, B.1    Rhind, N.2    Russell, P.3
  • 9
    • 0029079267 scopus 로고
    • Cell cycle regulation of the activity and subcellular localization of PLK1, 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 PLK1, 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
  • 11
    • 0024540118 scopus 로고
    • Sequence and mutational analysis of ESS 1, a gene essential for growth in Saccharomyces cerevisiae
    • Hanes, S.D., Shank, P.R. and Bostian, K.A. (1989) Sequence and mutational analysis of ESS 1, a gene essential for growth in Saccharomyces cerevisiae. Yeast, 5, 55-72.
    • (1989) Yeast , vol.5 , pp. 55-72
    • Hanes, S.D.1    Shank, P.R.2    Bostian, K.A.3
  • 12
    • 0029039470 scopus 로고
    • Phosphorylation and activation of the Xenopus Cdc25 phosphatase in the absence of Cdc2 and Cdk2 kinase activity
    • Izumi, T. and Maller, J.L. (1995) Phosphorylation and activation of the Xenopus Cdc25 phosphatase in the absence of Cdc2 and Cdk2 kinase activity. Mol. Biol. Cell, 6, 215-226.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 215-226
    • Izumi, T.1    Maller, J.L.2
  • 13
    • 0028216850 scopus 로고
    • Membrane localization of the kinase which phosphorylates p34Cdc2 on Threonine 14
    • Kornbluth, S., Sebastian, B., Hunter, T. and Newport, J. (1994) Membrane localization of the kinase which phosphorylates p34Cdc2 on Threonine 14. Mol. Biol. Cell., 5, 273-282.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 273-282
    • Kornbluth, S.1    Sebastian, B.2    Hunter, T.3    Newport, J.4
  • 14
    • 0026689359 scopus 로고
    • cdc2 phosphorylation site mutants: Effects upon cell cycle progression in the fission yeast Schizosaccharomyces pombe
    • cdc2 phosphorylation site mutants: effects upon cell cycle progression in the fission yeast Schizosaccharomyces 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
  • 15
    • 0026719599 scopus 로고
    • Regulation of the Cdc25 protein during the cell cycle in Xenopus extracts
    • Kumagai, A. and Dunphy, W.G. (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
  • 16
    • 0029821131 scopus 로고    scopus 로고
    • Purification and molecular cloning of Plx 1, a Cdc25-regulatory kinase from Xenopus egg extracts
    • Kumagai, A. and Dunphy, W.G. (1996) Purification and molecular cloning of Plx 1, 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
  • 17
    • 0030462914 scopus 로고    scopus 로고
    • Antibody micro injection reveals an essential role for human polo-like kinasel (Plk1) in the functional maturation of mitotic centrosomes
    • Lane, H.A. and Nigg, E.A. (1996) Antibody micro injection reveals an essential role for human polo-like kinasel (Plk1) in the functional maturation of mitotic centrosomes. J. Cell Biol., 135, 1701-1713.
    • (1996) J. Cell Biol. , vol.135 , pp. 1701-1713
    • Lane, H.A.1    Nigg, E.A.2
  • 18
    • 0028884602 scopus 로고
    • Plk1 is an M-phase-specific protein kinase and interacts with a kinesin-like protein, CHO-MKLP-1
    • Lee, K.S., Yuan, Y-L., Kuriyama, R. and Erikson, R. (1995) Plk1 is an M-phase-specific protein kinase and interacts with a kinesin-like protein, CHO-MKLP-1. Mol. Cell. Biol., 15, 7143-7151.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7143-7151
    • Lee, K.S.1    Yuan, Y.-L.2    Kuriyama, R.3    Erikson, R.4
  • 19
    • 0031053117 scopus 로고    scopus 로고
    • The human Myt1 kinase preferentially phosphorylates Cdc2 on Threonine 14 and localizes to the endoplasmic reticulum and golgi complex
    • Liu, F., Stanton, J.J., Wu, Z. and Piwnica-Worms, H. (1997) The human Myt1 kinase preferentially phosphorylates Cdc2 on Threonine 14 and localizes to the endoplasmic reticulum and golgi complex. Mol. Cell. Biol., 17, 571-583.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 571-583
    • Liu, F.1    Stanton, J.J.2    Wu, Z.3    Piwnica-Worms, H.4
  • 20
    • 0027512931 scopus 로고
    • Properties and regulation of the cell cycle-specific NIMA protein kinase of Aspergillus nidulans
    • Lu, K.P., Osmani, S.A. and Means, A.R. (1993) Properties and regulation of the cell cycle-specific NIMA protein kinase of Aspergillus nidulans. J. Biol. Chem., 268, 8769-8776.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8769-8776
    • Lu, K.P.1    Osmani, S.A.2    Means, A.R.3
  • 21
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu, K.P., Hanes, S.D. and Hunter, T. (1996) A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature, 380, 544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 22
    • 0030033395 scopus 로고    scopus 로고
    • The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae
    • Maleszka, R., Hanes, S.D., Hackett, R.L., de Couet, H.G. and Miklos, G.L. (1996) The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae. Proc. Natt Acad. Sci. USA, 93, 447-451.
    • (1996) Proc. Natt Acad. Sci. USA , vol.93 , pp. 447-451
    • Maleszka, R.1    Hanes, S.D.2    Hackett, R.L.3    De Couet, H.G.4    Miklos, G.L.5
  • 23
    • 0029000155 scopus 로고
    • Cell cycle regulation of human WEE1
    • McGowan, C.H. and Russell, P. (1995) Cell cycle regulation of human WEE1. EMBO J., 14, 2166-2175.
    • (1995) EMBO J. , vol.14 , pp. 2166-2175
    • McGowan, C.H.1    Russell, P.2
  • 24
    • 0026569665 scopus 로고
    • The Cdc25 M-phase inducer: An unconventional protein phosphatase
    • Millar, J.B.A. and Russell, P. (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
  • 25
    • 0016789438 scopus 로고
    • Mitotic mutants of Aspergillus nidulans
    • Morris, N.R. (1976) Mitotic mutants of Aspergillus nidulans. Genet. Res. Camb., 26, 237-254.
    • (1976) Genet. Res. Camb. , vol.26 , pp. 237-254
    • Morris, N.R.1
  • 26
    • 0028998865 scopus 로고
    • Cell cycle regulation of a Xenopus Wee1-like kinase
    • Mueller, P.R., Coleman, T.R. and Dunphy, W.G. (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
  • 27
    • 0028783413 scopus 로고
    • Myt1: A membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15
    • Mueller, P.R., Coleman, T.R., Kuamgai, A. and Dunphy, W.G. (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    Kuamgai, A.3    Dunphy, W.G.4
  • 28
    • 0024978338 scopus 로고
    • Cyclin synthesis drives the early embryonic cell cycle
    • Murray, A. and Kirschner, M. (1989) Cyclin synthesis drives the early embryonic cell cycle. Nature, 339, 275-280.
    • (1989) Nature , vol.339 , pp. 275-280
    • Murray, A.1    Kirschner, M.2
  • 29
    • 0024978344 scopus 로고
    • The role of cyclin synthesis and degradation in the control of MPF activity
    • Murray, A., Solomon, M.J. and Kirschner, M.W. (1989) The role of cyclin synthesis and degradation in the control of MPF activity. Nature, 339, 280-286.
    • (1989) Nature , vol.339 , pp. 280-286
    • Murray, A.1    Solomon, M.J.2    Kirschner, M.W.3
  • 31
    • 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
  • 33
    • 0024294395 scopus 로고
    • 2-specific gene that encodes a potential protein kinase
    • 2-specific gene that encodes a potential protein kinase. Cell, 53, 237-244.
    • (1988) Cell , vol.53 , pp. 237-244
    • Osmani, S.A.1    Pu, R.T.2    Morris, N.R.3
  • 34
    • 0025861473 scopus 로고
    • Activation of the nimA protein kinase plays a unique role during mitosis that cannot be bypassed by absence of the bimE checkpoint
    • Osmani, A.H., O'Donnell, K., Pu, R.T. and Osmani, S.A. (1991a) Activation of the nimA protein kinase plays a unique role during mitosis that cannot be bypassed by absence of the bimE checkpoint, EMBO J., 9, 2669-2679.
    • (1991) EMBO J. , vol.9 , pp. 2669-2679
    • Osmani, A.H.1    O'Donnell, K.2    Pu, R.T.3    Osmani, S.A.4
  • 35
    • 0026048594 scopus 로고
    • Cdc2 cell cycle-regulated protein kinases is required to initiate mitosis in
    • Cdc2 cell cycle-regulated protein kinases is required to initiate mitosis in A.nidulans. Cell, 67, 283-291.
    • (1991) A.nidulans. Cell , vol.67 , pp. 283-291
    • Osmani, A.H.1    McGuire, S.L.2    Osmani, S.A.3
  • 36
    • 0030611095 scopus 로고    scopus 로고
    • Mitotic and 62 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216
    • Peng, C.-Y., Graves, P.R., Thoma, R.S., Wu, Z., Shaw, A.S. and Piwnica-Worms, H. (1997) Mitotic and 62 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216. Science, 277, 1501-1505.
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.-Y.1    Graves, P.R.2    Thoma, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 37
    • 0028124244 scopus 로고
    • Confirmation of the existence of a third family of peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant protein production of parvulin
    • Rahfeld, J.U., Rucknagel, K.P., Schelbert, B., Ludwig, B., Hacker, J., Mann, K. and Fischer, G. (1994) Confirmation of the existence of a third family of peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant protein production of parvulin. Febs Lett., 352, 180-184.
    • (1994) Febs Lett. , vol.352 , pp. 180-184
    • Rahfeld, J.U.1    Rucknagel, K.P.2    Schelbert, B.3    Ludwig, B.4    Hacker, J.5    Mann, K.6    Fischer, G.7
  • 38
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan, R., Lu, K.P., Hunter, T. and Noel, J.P. (1997) Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell, 89, 875-886.
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 39
    • 0030867582 scopus 로고    scopus 로고
    • Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regulation through Cdc25
    • Sanchez, Y., Wong, C., Thoma, R.S., Richman, R., Wu, Z., Piwnica-Worms, H. and Elledge, S.J. (1997) Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regulation through Cdc25. Science, 277, 1497-1501.
    • (1997) Science , vol.277 , pp. 1497-1501
    • Sanchez, Y.1    Wong, C.2    Thoma, R.S.3    Richman, R.4    Wu, Z.5    Piwnica-Worms, H.6    Elledge, S.J.7
  • 40
    • 0029364576 scopus 로고
    • Prolyl isomerases join the fold
    • Schmid, F.X. (1995) Prolyl isomerases join the fold. Curr. Biol., 5, 993-994.
    • (1995) Curr. Biol. , vol.5 , pp. 993-994
    • Schmid, F.X.1
  • 41
    • 0026263951 scopus 로고
    • Systems for the study of nuclear assembly, DNA replication and nuclear breakdown in Xenopus laevis egg extracts
    • Smythe, C. and Newport, J.W. (1991) Systems for the study of nuclear assembly, DNA replication and nuclear breakdown in Xenopus laevis egg extracts. Methods Cell Biol., 35, 449-468.
    • (1991) Methods Cell Biol. , vol.35 , pp. 449-468
    • Smythe, C.1    Newport, J.W.2
  • 43
    • 0027587321 scopus 로고
    • Activation of the various cyclin/Cdc2 protein kinases
    • Solomon, M.J. (1993) Activation of the various cyclin/Cdc2 protein kinases. Curr. Opin. Cell Biol, 5, 180-186.
    • (1993) Curr. Opin. Cell Biol , vol.5 , pp. 180-186
    • Solomon, M.J.1
  • 47
    • 0030424581 scopus 로고    scopus 로고
    • Structure and function of the WW domain
    • Sudol, M. (1996) Structure and function of the WW domain. Prog. Biophys. Mol. Biol, 65, 113-132.
    • (1996) Prog. Biophys. Mol. Biol , vol.65 , pp. 113-132
    • Sudol, M.1
  • 48
    • 0029048491 scopus 로고
    • Regulation of the human Wee1Hu CDK tyrosine-15 kinase during the cell cycle
    • Watanabe, N., Broome, M. and Hunter, T. (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
  • 49
    • 0031438929 scopus 로고    scopus 로고
    • Sequence-specific and phosphorylation-dependent proline isomerization: A potential mitotic regulatory mechanism
    • Yaffe, M.B. et al. (1997). Sequence-specific and phosphorylation-dependent proline isomerization: A potential mitotic regulatory mechanism. Science, 278, 1957-1960.
    • (1997) Science , vol.278 , pp. 1957-1960
    • Yaffe, M.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.