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Volumn 24, Issue 3, 2004, Pages 1206-1218

ERF Nuclear Shuttling, a Continuous Monitor of Erk Activity That Liks It to Cell Cycle Progression

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; RETINOBLASTOMA PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ERF; UNCLASSIFIED DRUG;

EID: 1642580780     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.3.1206-1218.2004     Document Type: Article
Times cited : (58)

References (63)
  • 1
    • 0034610996 scopus 로고    scopus 로고
    • Nuclear export of MAP kinase (ERK) involves a MAP kinase kinase (MEK)-dependent active transport mechanism
    • Adachi, M., M. Fukuda, and E. Nishida. 2000. Nuclear export of MAP kinase (ERK) involves a MAP kinase kinase (MEK)-dependent active transport mechanism. J. Cell Biol. 148:849-856.
    • (2000) J. Cell Biol. , vol.148 , pp. 849-856
    • Adachi, M.1    Fukuda, M.2    Nishida, E.3
  • 2
    • 0033215340 scopus 로고    scopus 로고
    • Two co-existing mechanisms for nuclear import of MAP kinase: Passive diffusion of a monomer and active transport of a dimer
    • Adachi, M., M. Fukuda, and E. Nishida. 1999. Two co-existing mechanisms for nuclear import of MAP kinase: passive diffusion of a monomer and active transport of a dimer. EMBO J. 18:5347-5358.
    • (1999) EMBO J. , vol.18 , pp. 5347-5358
    • Adachi, M.1    Fukuda, M.2    Nishida, E.3
  • 3
    • 0037040984 scopus 로고    scopus 로고
    • p21 (Cip1) promotes cyclin D1 nuclear accumulation via direct inhibition of nuclear export
    • Alt, J. R., A. B. Gladden, and J. A. Diehl. 2002. p21 (Cip1) promotes cyclin D1 nuclear accumulation via direct inhibition of nuclear export. J. Biol. Chem. 277:8517-8523.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8517-8523
    • Alt, J.R.1    Gladden, A.B.2    Diehl, J.A.3
  • 4
    • 0035868386 scopus 로고    scopus 로고
    • The contribution of the acidic domain of MDM2 to p53 and MDM2 stability
    • Argentini, M., N. Barboule, and B. Wasylyk, 2001. The contribution of the acidic domain of MDM2 to p53 and MDM2 stability. Oncogene 20:1267-1275.
    • (2001) Oncogene , vol.20 , pp. 1267-1275
    • Argentini, M.1    Barboule, N.2    Wasylyk, B.3
  • 6
    • 0024294357 scopus 로고
    • Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-κB transcription factor
    • Baeuerle, P. A., and D. Baltimore. 1988. Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-κB transcription factor. Cell 53:211-217.
    • (1988) Cell , vol.53 , pp. 211-217
    • Baeuerle, P.A.1    Baltimore, D.2
  • 7
    • 0037323903 scopus 로고    scopus 로고
    • Regulation of cell survival and proliferation by the FOXO (Forkhead box, class O) subfamily of Forkhead transcription factors
    • Birkenkamp, K. U., and P. J. Coffer. 2003. Regulation of cell survival and proliferation by the FOXO (Forkhead box, class O) subfamily of Forkhead transcription factors. Biochem. Soc. Trans. 31:292-297.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 292-297
    • Birkenkamp, K.U.1    Coffer, P.J.2
  • 8
    • 0035856514 scopus 로고    scopus 로고
    • DNA binding domains in diverse nuclear receptors function as nuclear export signals
    • Black, B. E., J. M. Holaska, F. Rastinejad, and B. M. Paschal. 2001. DNA binding domains in diverse nuclear receptors function as nuclear export signals. Curr. Biol. 11:1749-1758.
    • (2001) Curr. Biol. , vol.11 , pp. 1749-1758
    • Black, B.E.1    Holaska, J.M.2    Rastinejad, F.3    Paschal, B.M.4
  • 9
    • 0024331611 scopus 로고
    • Definition of an Ets1 protein domain required for nuclear localization in cells and DNA-binding activity in vitro
    • Boulukos, K. E., P. Pognonec, B. Rabault, A. Begue, and J. Ghysdael. 1989. Definition of an Ets1 protein domain required for nuclear localization in cells and DNA-binding activity in vitro. Mol. Cell. Biol. 9:5718-5721.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5718-5721
    • Boulukos, K.E.1    Pognonec, P.2    Rabault, B.3    Begue, A.4    Ghysdael, J.5
  • 11
    • 0030706186 scopus 로고    scopus 로고
    • Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway
    • Chow, C. W., M. Rincon, J. Cavanagh, M. Dickens, and R. J. Davis. 1997. Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway. Science 278:1638-1641.
    • (1997) Science , vol.278 , pp. 1638-1641
    • Chow, C.W.1    Rincon, M.2    Cavanagh, J.3    Dickens, M.4    Davis, R.J.5
  • 12
    • 0033599014 scopus 로고    scopus 로고
    • ERK activation induces phosphotylation of Elk-1 at multiple S/T-P motifs to high stoichiometry
    • Cruzalegui, F. H., E. Cano, and R. Treisman. 1999. ERK activation induces phosphotylation of Elk-1 at multiple S/T-P motifs to high stoichiometry. Oncogene 18:7948-7957.
    • (1999) Oncogene , vol.18 , pp. 7948-7957
    • Cruzalegui, F.H.1    Cano, E.2    Treisman, R.3
  • 13
    • 0036901897 scopus 로고    scopus 로고
    • Loss of Rb overrides the requirement for ERK activity for cell proliferation
    • D'Abaco, G. M., S. Hooper, H. Paterson, and C. J. Marshall. 2002. Loss of Rb overrides the requirement for ERK activity for cell proliferation. J. Cell Sci. 115:4607-4616.
    • (2002) J. Cell Sci. , vol.115 , pp. 4607-4616
    • D'Abaco, G.M.1    Hooper, S.2    Paterson, H.3    Marshall, C.J.4
  • 14
    • 0032825496 scopus 로고    scopus 로고
    • The net repressor is regulated by nuclear export in response to anisomycin, UV, and heat shock
    • Ducret, C., S. M. Maira, A. Dierich, and B. Wasylyk. 1999. The net repressor is regulated by nuclear export in response to anisomycin, UV, and heat shock. Mol. Cell. Biol. 19:7076-7087.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7076-7087
    • Ducret, C.1    Maira, S.M.2    Dierich, A.3    Wasylyk, B.4
  • 15
    • 0035854645 scopus 로고    scopus 로고
    • Nuclear export of human beta-catenin can occur independent of CRM1 and the adenomatous polyposis coli tumor suppressor
    • Eleftheriou, A., M. Yoshida, and B. R. Henderson. 2001. Nuclear export of human beta-catenin can occur independent of CRM1 and the adenomatous polyposis coli tumor suppressor. J. Biol. Chem. 276:25883-25888.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25883-25888
    • Eleftheriou, A.1    Yoshida, M.2    Henderson, B.R.3
  • 16
    • 0037440429 scopus 로고    scopus 로고
    • Regulation of tumor suppressors by nuclear-cytoplasmic shuttling
    • Fabbro, M., and B. R. Henderson. 2003. Regulation of tumor suppressors by nuclear-cytoplasmic shuttling. Exp. Cell Res. 282:59-69.
    • (2003) Exp. Cell Res. , vol.282 , pp. 59-69
    • Fabbro, M.1    Henderson, B.R.2
  • 17
    • 0030830220 scopus 로고    scopus 로고
    • Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins
    • Frost, J. A., H. Steen, P. Shapiro, T. Lewis, N. Ahn, P. E. Shaw, and M. H. Cobb. 1997. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J. 16:6426-6438.
    • (1997) EMBO J. , vol.16 , pp. 6426-6438
    • Frost, J.A.1    Steen, H.2    Shapiro, P.3    Lewis, T.4    Ahn, N.5    Shaw, P.E.6    Cobb, M.H.7
  • 18
    • 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
  • 19
    • 0035313546 scopus 로고    scopus 로고
    • Nuclear shuttling of mitogen-activated protein (MAP) kinase (extracellular signal-regulated kinase (ERK) 2) was dynamically controlled by MAP/ERK kinase after antigen stimulation in RBL-2H3 cells
    • Furuno, T., N. Hirashima, S. Onizawa, N. Sagiya, and M. Nakanishi. 2001. Nuclear shuttling of mitogen-activated protein (MAP) kinase (extracellular signal-regulated kinase (ERK) 2) was dynamically controlled by MAP/ERK kinase after antigen stimulation in RBL-2H3 cells. J. Immunol. 166:4416-4421.
    • (2001) J. Immunol. , vol.166 , pp. 4416-4421
    • Furuno, T.1    Hirashima, N.2    Onizawa, S.3    Sagiya, N.4    Nakanishi, M.5
  • 20
    • 0035827321 scopus 로고    scopus 로고
    • The rules and roles of nucleocytoplasmic shuttling proteins
    • Gama-Carvalho, M., and M. Carmo-Fonseca. 2001. The rules and roles of nucleocytoplasmic shuttling proteins. FEBS Lett. 498:157-163.
    • (2001) FEBS Lett. , vol.498 , pp. 157-163
    • Gama-Carvalho, M.1    Carmo-Fonseca, M.2
  • 21
    • 0032557579 scopus 로고    scopus 로고
    • An analysis of Mek1 signaling in cell proliferation and transformation
    • Greulich, H., and R. L. Erikson. 1998. An analysis of Mek1 signaling in cell proliferation and transformation. J. Biol. Chem. 273:13280-13288.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13280-13288
    • Greulich, H.1    Erikson, R.L.2
  • 22
    • 0035196861 scopus 로고    scopus 로고
    • Identification of p53 sequence elements that are required for MDM2-mediated nuclear export
    • Gu, J., L. Nie, D. Wiederschain, and Z. M. Yuan. 2001. Identification of p53 sequence elements that are required for MDM2-mediated nuclear export. Mol. Cell. Biol. 21:8533-8546.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8533-8546
    • Gu, J.1    Nie, L.2    Wiederschain, D.3    Yuan, Z.M.4
  • 23
    • 0035930616 scopus 로고    scopus 로고
    • Intracellular localization of the Ret finger protein depends on a functional nuclear export signal and protein kinase C activation
    • Harbers, M., T. Nomura, S. Ohno, and S. Ishii. 2001. Intracellular localization of the Ret finger protein depends on a functional nuclear export signal and protein kinase C activation. J. Biol. Chem. 276:48596-48607.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48596-48607
    • Harbers, M.1    Nomura, T.2    Ohno, S.3    Ishii, S.4
  • 24
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals
    • Henderson, B. R., and A. Eleftheriou. 2000. A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals. Exp. Cell Res. 256:213-224.
    • (2000) Exp. Cell Res. , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 25
    • 0033537968 scopus 로고    scopus 로고
    • Regulation of DNA binding activity and nuclear transport of B-Myb in Xenopus oocytes
    • Humbert-Lan, G., and T. Pieler. 1999. Regulation of DNA binding activity and nuclear transport of B-Myb in Xenopus oocytes. J. Biol. Chem. 274:10293-10300.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10293-10300
    • Humbert-Lan, G.1    Pieler, T.2
  • 26
    • 0036343646 scopus 로고    scopus 로고
    • Nuclear localization of the tight junction protein ZO-2 in epithelial cells
    • Islas, S., J. Vega, L. Ponce, and L. Gonzalez-Mariscal. 2002. Nuclear localization of the tight junction protein ZO-2 in epithelial cells. Exp. Cell Res. 274:138-148.
    • (2002) Exp. Cell Res. , vol.274 , pp. 138-148
    • Islas, S.1    Vega, J.2    Ponce, L.3    Gonzalez-Mariscal, L.4
  • 27
    • 0036201059 scopus 로고    scopus 로고
    • Cyclin A- and cyclin E-Cdk complexes shuttle between the nucleus and the cytoplasm
    • Jackman, M., Y. Kubota, N. den Elzen, A. Hagting, and J. Pines. 2002. Cyclin A- and cyclin E-Cdk complexes shuttle between the nucleus and the cytoplasm. Mol. Biol. Cell 13:1030-1045.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1030-1045
    • Jackman, M.1    Kubota, Y.2    Den Elzen, N.3    Hagting, A.4    Pines, J.5
  • 28
    • 0034041537 scopus 로고    scopus 로고
    • Nuclear targeting signal recognition: A key control point in nuclear transport?
    • Jans, D. A., C. Y. Xiao, and M. H. Lam. 2000. Nuclear targeting signal recognition: a key control point in nuclear transport? Bioessays 22:532-544.
    • (2000) Bioessays , vol.22 , pp. 532-544
    • Jans, D.A.1    Xiao, C.Y.2    Lam, M.H.3
  • 32
    • 0033050069 scopus 로고    scopus 로고
    • Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation
    • Le Gallic, L., D. Sgouras, G. Beal, Jr., and G. Mavrothalassitis. 1999. Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation. Mol. Cell. Biol. 19:4121-4133.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4121-4133
    • Le Gallic, L.1    Sgouras, D.2    Beal Jr., G.3    Mavrothalassitis, G.4
  • 33
    • 0037439199 scopus 로고    scopus 로고
    • MAP kinase phosphorylation-dependent activation of Elk-1 leads to activation of the co-activator p300
    • Li, Q. J., S. H. Yang, Y. Maeda, F. M. Sladek, A. D. Sharrocks, and M. Martins-Green. 2003. MAP kinase phosphorylation-dependent activation of Elk-1 leads to activation of the co-activator p300. EMBO J. 22:281-291.
    • (2003) EMBO J. , vol.22 , pp. 281-291
    • Li, Q.J.1    Yang, S.H.2    Maeda, Y.3    Sladek, F.M.4    Sharrocks, A.D.5    Martins-Green, M.6
  • 34
    • 0037183703 scopus 로고    scopus 로고
    • Activation of Go-coupled dopamine D2 receptors inhibits ERK1/ERK2 in pituitary cells. A key step in the transcriptional suppression of the prolactin gene
    • Liu, J. C., R. E. Baker, C. Sun, V. C. Sundmark, and H. P. Elsholtz. 2002. Activation of Go-coupled dopamine D2 receptors inhibits ERK1/ERK2 in pituitary cells. A key step in the transcriptional suppression of the prolactin gene. J. Biol. Chem. 277:35819-35825.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35819-35825
    • Liu, J.C.1    Baker, R.E.2    Sun, C.3    Sundmark, V.C.4    Elsholtz, H.P.5
  • 35
    • 0035976962 scopus 로고    scopus 로고
    • IκBβ, but not IκBα, functions as a classical cytoplasmic inhibitor of NF-κB dimers by masking both NF-κB nuclear localization sequences in resting cells
    • Malek, S., Y. Chen, T. Huxford, and G. Ghosh. 2001. IκBβ, but not IκBα, functions as a classical cytoplasmic inhibitor of NF-κB dimers by masking both NF-κB nuclear localization sequences in resting cells. J. Biol. Chem. 276:45225-45235.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45225-45235
    • Malek, S.1    Chen, Y.2    Huxford, T.3    Ghosh, G.4
  • 36
    • 0034684622 scopus 로고    scopus 로고
    • Proteins of the ETS family with transcriptional repressor activity
    • Mavrothalassitis, G., and J. Ghysdael. 2000. Proteins of the ETS family with transcriptional repressor activity. Oncogene 19:6524-6532.
    • (2000) Oncogene , vol.19 , pp. 6524-6532
    • Mavrothalassitis, G.1    Ghysdael, J.2
  • 37
    • 0037020266 scopus 로고    scopus 로고
    • Structure of mitogen-activated protein kinase-activated protein (MAPKAP) kinase 2 suggests a bifunctional switch that couples kinase activation with nuclear export
    • Meng, W., L. L. Swenson, M. J. Fitzgibbon, K. Hayakawa, E. Ter Haar, A. E. Behrens, J. R. Fulghum, and J. A. Lippke. 2002. Structure of mitogen-activated protein kinase-activated protein (MAPKAP) kinase 2 suggests a bifunctional switch that couples kinase activation with nuclear export. J. Biol. Chem. 277:37401-37405.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37401-37405
    • Meng, W.1    Swenson, L.L.2    Fitzgibbon, M.J.3    Hayakawa, K.4    Ter Haar, E.5    Behrens, A.E.6    Fulghum, J.R.7    Lippke, J.A.8
  • 38
    • 0030978415 scopus 로고    scopus 로고
    • The K nuclear shuttling domain: A novel signal for nuclear import and nuclear export in the hnRNP K protein
    • Michael, W. M., P. S. Eder, and G. Dreyfuss. 1997. The K nuclear shuttling domain: a novel signal for nuclear import and nuclear export in the hnRNP K protein. EMBO J. 16:3587-3598.
    • (1997) EMBO J. , vol.16 , pp. 3587-3598
    • Michael, W.M.1    Eder, P.S.2    Dreyfuss, G.3
  • 39
    • 0031105404 scopus 로고    scopus 로고
    • Ras signalling is required for inactivation of the tumour suppressor pRb cell-cycle control protein
    • Mittnacht, S., H. Paterson, M. F. Olson, and C. J. Marshall. 1997. Ras signalling is required for inactivation of the tumour suppressor pRb cell-cycle control protein. Curr. Biol. 7:219-221.
    • (1997) Curr. Biol. , vol.7 , pp. 219-221
    • Mittnacht, S.1    Paterson, H.2    Olson, M.F.3    Marshall, C.J.4
  • 40
    • 0034528346 scopus 로고    scopus 로고
    • 14-3-3 Proteins: Regulation of subcellular localization by molecular interference
    • Muslin, A. J., and H. Xing. 2000. 14-3-3 proteins: regulation of subcellular localization by molecular interference. Cell. Signal. 12:703-709.
    • (2000) Cell. Signal. , vol.12 , pp. 703-709
    • Muslin, A.J.1    Xing, H.2
  • 41
    • 0028239896 scopus 로고
    • The activities of two Ets-related transcription factors required for Drosophila eye development are modulated by the Ras/MAPK pathway
    • O'Neill, E. M., I. Rebay, R. Tjian, and G. M. Rubin. 1994. The activities of two Ets-related transcription factors required for Drosophila eye development are modulated by the Ras/MAPK pathway. Cell 78:137-147.
    • (1994) Cell , vol.78 , pp. 137-147
    • O'Neill, E.M.1    Rebay, I.2    Tjian, R.3    Rubin, G.M.4
  • 44
    • 0035802117 scopus 로고    scopus 로고
    • Calcineurin-dependent nuclear import of the transcription factor Crz1p requires Nmd5p
    • Polizotto, R. S., and M. S. Cyert. 2001. Calcineurin-dependent nuclear import of the transcription factor Crz1p requires Nmd5p. J. Cell Biol. 154:951-960.
    • (2001) J. Cell Biol. , vol.154 , pp. 951-960
    • Polizotto, R.S.1    Cyert, M.S.2
  • 45
    • 0034680440 scopus 로고    scopus 로고
    • IκBα and IκBα/NF-κB complexes are retained in the cytoplasm through interaction with a novel partner, RasGAP SH3-binding protein 2
    • Prigent, M., I. Barlat, H. Langen, and C. Dargemont. 2000. IκBα and IκBα/NF-κB complexes are retained in the cytoplasm through interaction with a novel partner, RasGAP SH3-binding protein 2. J. Biol. Chem. 275:36441-36449.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36441-36449
    • Prigent, M.1    Barlat, I.2    Langen, H.3    Dargemont, C.4
  • 46
    • 0036312041 scopus 로고    scopus 로고
    • Sox10 is an active nucleocytoplasmic shuttle protein, and shuttling is crucial for Sox10-mediated transactivation
    • Rehberg, S., P. Lischka, G. Glaser, T. Stamminger, M. Wegner, and O. Rosorius. 2002. Sox10 is an active nucleocytoplasmic shuttle protein, and shuttling is crucial for Sox10-mediated transactivation. Mol. Cell. Biol. 22:5826-5834.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5826-5834
    • Rehberg, S.1    Lischka, P.2    Glaser, G.3    Stamminger, T.4    Wegner, M.5    Rosorius, O.6
  • 48
    • 0033180582 scopus 로고    scopus 로고
    • Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding
    • Rittinger, K., J. Budman, J. Xu, S. Volinia, L. C. Cantley, S. J. Smerdon, S. J. Gamblin, and M. B. Yaffe. 1999. Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol. Cell 4:153-166.
    • (1999) Mol. Cell , vol.4 , pp. 153-166
    • Rittinger, K.1    Budman, J.2    Xu, J.3    Volinia, S.4    Cantley, L.C.5    Smerdon, S.J.6    Gamblin, S.J.7    Yaffe, M.B.8
  • 50
    • 0028009754 scopus 로고
    • Dual control of myc expression through a single DNA binding site targeted by ets family proteins and E2F-1
    • Roussel, M. F., J. N. Davis, J. L. Cleveland, J. Ghysdael, and S. W. Hiebert. 1994. Dual control of myc expression through a single DNA binding site targeted by ets family proteins and E2F-1. Oncogene 9:405-415.
    • (1994) Oncogene , vol.9 , pp. 405-415
    • Roussel, M.F.1    Davis, J.N.2    Cleveland, J.L.3    Ghysdael, J.4    Hiebert, S.W.5
  • 52
    • 0029095176 scopus 로고
    • ERF: An ETS domain protein with strong transcriptional repressor activity, can suppress ets-associated tumorigenesis and is regulated by phosphorylation during cell cycle and mitogenic stimulation
    • Sgouras, D. N., M. A. Athanasiou, G. J. Beal, Jr., R. J. Fisher, D. G. Blair, and G. J. Mavrothalassitis. 1995. ERF: an ETS domain protein with strong transcriptional repressor activity, can suppress ets-associated tumorigenesis and is regulated by phosphorylation during cell cycle and mitogenic stimulation. EMBO J. 14:4781-4793.
    • (1995) EMBO J. , vol.14 , pp. 4781-4793
    • Sgouras, D.N.1    Athanasiou, M.A.2    Beal Jr., G.J.3    Fisher, R.J.4    Blair, D.G.5    Mavrothalassitis, G.J.6
  • 53
    • 0033559256 scopus 로고    scopus 로고
    • A leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localization and p53 activity by NES masking
    • Stommel, J. M., N. D. Marchenko, G. S. Jimenez, U. M. Moll, T. J. Hope, and G. M. Wahl. 1999. A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking. EMBO J. 18:1660-1672.
    • (1999) EMBO J. , vol.18 , pp. 1660-1672
    • Stommel, J.M.1    Marchenko, N.D.2    Jimenez, G.S.3    Moll, U.M.4    Hope, T.J.5    Wahl, G.M.6
  • 54
    • 0037199975 scopus 로고    scopus 로고
    • The coiled coil region (amino acids 129-250) of the tumor suppressor protein adenomatous polyposis coli (APC). Its structure and its interaction with chromosome maintenance region 1 (Crm-1)
    • Tickenbrock, L., J. Cramer, I. R. Vetter, and O. Muller. 2002. The coiled coil region (amino acids 129-250) of the tumor suppressor protein adenomatous polyposis coli (APC). Its structure and its interaction with chromosome maintenance region 1 (Crm-1). J. Biol. Chem. 277:32332-32338.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32332-32338
    • Tickenbrock, L.1    Cramer, J.2    Vetter, I.R.3    Muller, O.4
  • 55
    • 0034960921 scopus 로고    scopus 로고
    • Armadillo nuclear import is regulated by cytoplasmic anchor Axin and nuclear anchor dTCF/Pan
    • Tolwinski, N. S., and E. Wieschaus. 2001. Armadillo nuclear import is regulated by cytoplasmic anchor Axin and nuclear anchor dTCF/Pan. Development 128:2107-2117.
    • (2001) Development , vol.128 , pp. 2107-2117
    • Tolwinski, N.S.1    Wieschaus, E.2
  • 56
    • 0037348614 scopus 로고    scopus 로고
    • CRM1-mediated nuclear export and regulated activity of the receptor tyrosine kinase antagonist YAN require specific interactions with MAE
    • Tontle, T. L., P. S. Lee, and I. Rebay. 2003. CRM1-mediated nuclear export and regulated activity of the receptor tyrosine kinase antagonist YAN require specific interactions with MAE. Development 130:845-857.
    • (2003) Development , vol.130 , pp. 845-857
    • Tontle, T.L.1    Lee, P.S.2    Rebay, I.3
  • 57
    • 0029883919 scopus 로고    scopus 로고
    • ETS1 and ETS2 in p53 regulation: Spatial separation of ETS binding sites (EBS) modulate protein: DNA interaction
    • Venanzoni, M. C., L. R. Robinson, D. R. Hodge, I. Kola, and A. Seth. 1996. ETS1 and ETS2 in p53 regulation: Spatial separation of ETS binding sites (EBS) modulate protein: DNA interaction. Oncogene 12:1199-1204.
    • (1996) Oncogene , vol.12 , pp. 1199-1204
    • Venanzoni, M.C.1    Robinson, L.R.2    Hodge, D.R.3    Kola, I.4    Seth, A.5
  • 59
    • 0034450953 scopus 로고    scopus 로고
    • The Raf signal transduction cascade as a target for chemotherapeutic intervention in growth factor-responsive tumors
    • Weinstein-Oppenheimer, C. R., W. L. Blalock, L. S. Steelman, F. Chang, and J. A. McCubrey. 2000. The Raf signal transduction cascade as a target for chemotherapeutic intervention in growth factor-responsive tumors. Pharmacol. Ther. 88:229-279.
    • (2000) Pharmacol. Ther. , vol.88 , pp. 229-279
    • Weinstein-Oppenheimer, C.R.1    Blalock, W.L.2    Steelman, L.S.3    Chang, F.4    McCubrey, J.A.5
  • 60
    • 0347664883 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of Smad1 conferred by its nuclear localization and nuclear export signals
    • Xiao, Z., N. Watson, C. Rodriguez, and H. F. Lodish. 2001. Nucleocytoplasmic shuttling of Smad1 conferred by its nuclear localization and nuclear export signals. J. Biol. Chem. 276:39404-39410.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39404-39410
    • Xiao, Z.1    Watson, N.2    Rodriguez, C.3    Lodish, H.F.4
  • 61
    • 0036670359 scopus 로고    scopus 로고
    • Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFβ signaling complexes in the cytoplasm and nucleus
    • Xu, L., Y. Kang, S. Col, and J. Massague. 2002. Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFβ signaling complexes in the cytoplasm and nucleus. Mol. Cell 10:271-282.
    • (2002) Mol. Cell , vol.10 , pp. 271-282
    • Xu, L.1    Kang, Y.2    Col, S.3    Massague, J.4
  • 62
    • 0035076262 scopus 로고    scopus 로고
    • Temporal recruitment of the mSin3A-histone deacetylase corepressor complex to the ETS domain transcription factor Elk-1
    • Yang, S. H., E. Viekers, A. Brehm, T. Kouzarides, and A. D. Sharrocks. 2001. Temporal recruitment of the mSin3A-histone deacetylase corepressor complex to the ETS domain transcription factor Elk-1. Mol. Cell. Biol. 21:2802-2814.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2802-2814
    • Yang, S.H.1    Viekers, E.2    Brehm, A.3    Kouzarides, T.4    Sharrocks, A.D.5
  • 63
    • 0034684620 scopus 로고    scopus 로고
    • Signal transduction and the Ets family of transcription factors
    • Yordy, J. S., and R. C. Muise-Helmericks. 2000. Signal transduction and the Ets family of transcription factors. Oncogene 19:6503-6513.
    • (2000) Oncogene , vol.19 , pp. 6503-6513
    • Yordy, J.S.1    Muise-Helmericks, R.C.2


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