메뉴 건너뛰기




Volumn 24, Issue 5, 2010, Pages 1454-1466

The BRCA-1 binding protein BRAP2 is a novel, negative regulator of nuclear import of viral proteins, dependent on phosphorylation flanking the nuclear localization signal

Author keywords

Cytomegalovirus processivity factor ppUL44; Cytoplasmic retention factor; Nuclear transport regulation; p53 tumor suppressor; SV40 large tumor antigen; T ag

Indexed keywords

ALANINE; ASPARTIC ACID; BINDING PROTEIN; COLECALCIFEROL; CYCLIN DEPENDENT KINASE; DNA POLYMERASE; GREEN FLUORESCENT PROTEIN; HETERODIMER; PROTEIN BRAP2; PROTEIN P53; TRANSACTIVATOR PROTEIN; TUMOR ANTIGEN; UNCLASSIFIED DRUG; BRAP PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE; VIRUS PROTEIN; VIRUS T ANTIGEN;

EID: 77952294068     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-136564     Document Type: Article
Times cited : (35)

References (56)
  • 1
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich, D., and Kutay, U. (1999) Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15, 607-660
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 2
    • 0034041537 scopus 로고    scopus 로고
    • Nuclear targeting signal recognition a key control point in nuclear transport?
    • Jans, D. A., Xiao, C. Y., and Lam, M. H. (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
  • 3
    • 14544272335 scopus 로고    scopus 로고
    • Regulation of nuclear transport: Central role in development and transformation?
    • Poon, I. K., and Jans, D. A. (2005) Regulation of nuclear transport: central role in development and transformation? Traffic 6, 173-186
    • (2005) Traffic , vol.6 , pp. 173-186
    • Poon, I.K.1    Jans, D.A.2
  • 4
    • 0033279823 scopus 로고    scopus 로고
    • Regulation of nuclear localization: A key to a door
    • Kaffman, A., and O'Shea, E. K. (1999) Regulation of nuclear localization: a key to a door. Annu. Rev. Cell Dev. Biol. 15, 291-339
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 291-339
    • Kaffman, A.1    O'Shea, E.K.2
  • 5
    • 26944433406 scopus 로고    scopus 로고
    • A protein kinase CK2 site flanking the nuclear targeting signal enhances nuclear transport of human cytomegalovirus ppUL44
    • Alvisi, G., Jans, D. A., Guo, J., Pinna, L. A., and Ripalti, A. (2005) A protein kinase CK2 site flanking the nuclear targeting signal enhances nuclear transport of human cytomegalovirus ppUL44. Traffic 6, 1002-1013
    • (2005) Traffic , vol.6 , pp. 1002-1013
    • Alvisi, G.1    Jans, D.A.2    Guo, J.3    Pinna, L.A.4    Ripalti, A.5
  • 6
    • 38149089542 scopus 로고    scopus 로고
    • Regulated nucleocytoplasmic trafficking of viral gene products: A therapeutic target?
    • Alvisi, G., Rawlinson, S. M., Ghildyal, R., Ripalti, A., and Jans, D. A. (2008) Regulated nucleocytoplasmic trafficking of viral gene products: a therapeutic target? Biochim. Biophys. Acta 1784, 213-227
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 213-227
    • Alvisi, G.1    Rawlinson, S.M.2    Ghildyal, R.3    Ripalti, A.4    Jans, D.A.5
  • 7
    • 0026783210 scopus 로고
    • IκB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention
    • Beg, A. A., Ruben, S. M., Scheinman, R. I., Haskill, S., Rosen, C. A., and Baldwin, A. S., Jr. (1992) IκB interacts with the nuclear localization sequences of the subunits of NF-κB: a mechanism for cytoplasmic retention. Genes Dev. 6, 1899-1913
    • (1992) Genes Dev. , vol.6 , pp. 1899-1913
    • Beg, A.A.1    Ruben, S.M.2    Scheinman, R.I.3    Haskill, S.4    Rosen, C.A.5    Baldwin Jr., A.S.6
  • 8
    • 2442688987 scopus 로고    scopus 로고
    • Regulation of nuclear import by phosphorylation adjacent to nuclear localization signals
    • Harreman, M. T., Kline, T. M., Milford, H. G., Harben, M. B., Hodel, A. E., and Corbett, A. H. (2004) Regulation of nuclear import by phosphorylation adjacent to nuclear localization signals. J. Biol. Chem. 279, 20613-20621
    • (2004) J. Biol. Chem. , vol.279 , pp. 20613-20621
    • Harreman, M.T.1    Kline, T.M.2    Milford, H.G.3    Harben, M.B.4    Hodel, A.E.5    Corbett, A.H.6
  • 9
    • 0039468008 scopus 로고    scopus 로고
    • The protein kinase CK2 site (Ser111/112) enhances recognition of the simian virus 40 large T-antigen nuclear localization sequence by importin
    • Hubner, S., Xiao, C. Y., and Jans, D. A. (1997) The protein kinase CK2 site (Ser111/112) enhances recognition of the simian virus 40 large T-antigen nuclear localization sequence by importin. J. Biol. Chem. 272, 17191-17195
    • (1997) J. Biol. Chem. , vol.272 , pp. 17191-17195
    • Hubner, S.1    Xiao, C.Y.2    Jans, D.A.3
  • 10
    • 0025919717 scopus 로고
    • P34cdc2-mediated phosphorylation at T124 inhibits nuclear import of SV-40 T antigen proteins
    • Jans, D. A., Ackermann, M. J., Bischoff, J. R., Beach, D. H., and Peters, R. (1991) p34cdc2-mediated phosphorylation at T124 inhibits nuclear import of SV-40 T antigen proteins. J. Cell Biol. 115, 1203-1212
    • (1991) J. Cell Biol. , vol.115 , pp. 1203-1212
    • Jans, D.A.1    Ackermann, M.J.2    Bischoff, J.R.3    Beach, D.H.4    Peters, R.5
  • 11
    • 0029146850 scopus 로고
    • Cyclindependent kinase site-regulated signal-dependent nuclear localization of the SW15 yeast transcription factor in mammalian cells
    • Jans, D. A., Moll, T., Nasmyth, K., and Jans, P. (1995) Cyclindependent kinase site-regulated signal-dependent nuclear localization of the SW15 yeast transcription factor in mammalian cells. J. Biol. Chem. 270, 17064-17067
    • (1995) J. Biol. Chem. , vol.270 , pp. 17064-17067
    • Jans, D.A.1    Moll, T.2    Nasmyth, K.3    Jans, P.4
  • 12
    • 0032168565 scopus 로고    scopus 로고
    • Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121
    • Kaffman, A., Rank, N. M., and O'Shea, E. K. (1998) Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121. Genes Dev. 12, 2673-2683 (Pubitemid 28420648)
    • (1998) Genes and Development , vol.12 , Issue.17 , pp. 2673-2683
    • Kaffman, A.1    Rank, N.M.2    O'Shea, E.K.3
  • 13
    • 0033532281 scopus 로고    scopus 로고
    • Roles of phosphorylation sites in regulating activity of the transcription factor Pho4
    • Komeili, A., and O'Shea, E. K. (1999) Roles of phosphorylation sites in regulating activity of the transcription factor Pho4. Science 284, 977-980
    • (1999) Science , vol.284 , pp. 977-980
    • Komeili, A.1    O'Shea, E.K.2
  • 14
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-kappaB and stabilizes a newly phosphorylated form of IκB-alpha that is still bound to NF-κB
    • Traenckner, E. B., Wilk, S., and Baeuerle, P. A. (1994) A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I κB-alpha that is still bound to NF-κB. EMBO J. 13, 5433-5441 (Pubitemid 24351822)
    • (1994) EMBO Journal , vol.13 , Issue.22 , pp. 5433-5441
    • Traenckner, E.B.-M.1    Wilk, S.2    Baeuerle, P.A.3
  • 15
    • 1842330324 scopus 로고    scopus 로고
    • SV40 large tumor antigen nuclear import is regulated by the double-stranded DNA-dependent protein kinase site (serine 120) flanking the nuclear localization sequence
    • Xiao, C. Y., Hubner, S., and Jans, D. A. (1997) SV40 large tumor antigen nuclear import is regulated by the double-stranded DNA-dependent protein kinase site (serine 120) flanking the nuclear localization sequence. J. Biol. Chem. 272, 22191-22198
    • (1997) J. Biol. Chem. , vol.272 , pp. 22191-22198
    • Xiao, C.Y.1    Hubner, S.2    Jans, D.A.3
  • 16
    • 0032575492 scopus 로고    scopus 로고
    • The cAMP-dependent protein kinase site (Ser312) enhances dorsal nuclear import through facilitating nuclear localization sequence/importin interaction
    • Briggs, L. J., Stein, D., Goltz, J., Corrigan, V. C., Efthymiadis, A., Hubner, S., and Jans, D. A. (1998) The cAMP-dependent protein kinase site (Ser312) enhances dorsal nuclear import through facilitating nuclear localization sequence/importin interaction. J. Biol. Chem. 273, 22745-22752
    • (1998) J. Biol. Chem. , vol.273 , pp. 22745-22752
    • Briggs, L.J.1    Stein, D.2    Goltz, J.3    Corrigan, V.C.4    Efthymiadis, A.5    Hubner, S.6    Jans, D.A.7
  • 17
    • 1142297674 scopus 로고    scopus 로고
    • Regulation of nuclear retention of glucocorticoid receptor by nuclear Hsp90
    • Tago, K., Tsukahara, F., Naruse, M., Yoshioka, T., and Takano, K. (2004) Regulation of nuclear retention of glucocorticoid receptor by nuclear Hsp90. Mol. Cell. Endocrinol. 213, 131-138
    • (2004) Mol. Cell. Endocrinol. , vol.213 , pp. 131-138
    • Tago, K.1    Tsukahara, F.2    Naruse, M.3    Yoshioka, T.4    Takano, K.5
  • 18
    • 0032513113 scopus 로고    scopus 로고
    • Identification of a novel cytoplasmic protein that specifically binds to nuclear localization signal motifs
    • Li, S., Ku, C. Y., Farmer, A. A., Cong, Y. S., Chen, C. F., and Lee, W. H. (1998) Identification of a novel cytoplasmic protein that specifically binds to nuclear localization signal motifs. J. Biol. Chem. 273, 6183-6189
    • (1998) J. Biol. Chem. , vol.273 , pp. 6183-6189
    • Li, S.1    Ku, C.Y.2    Farmer, A.A.3    Cong, Y.S.4    Chen, C.F.5    Lee, W.H.6
  • 19
    • 4444285374 scopus 로고    scopus 로고
    • Brap2 functions as a cytoplasmic retention protein for p21 during monocyte differentiation
    • Asada, M., Ohmi, K., Delia, D., Enosawa, S., Suzuki, S., Yuo, A., Suzuki, H., and Mizutani, S. (2004) Brap2 functions as a cytoplasmic retention protein for p21 during monocyte differentiation. Mol. Cell. Biol. 24, 8236-8243
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8236-8243
    • Asada, M.1    Ohmi, K.2    Delia, D.3    Enosawa, S.4    Suzuki, S.5    Yuo, A.6    Suzuki, H.7    Mizutani, S.8
  • 20
    • 0026026630 scopus 로고
    • The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen
    • Rihs, H. P., Jans, D. A., Fan, H., and Peters, R. (1991) The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J. 10, 633-639 (Pubitemid 21905517)
    • (1991) EMBO Journal , vol.10 , Issue.3 , pp. 633-639
    • Rihs, H.-P.1    Jans, D.A.2    Fan, H.3    Peters, R.4
  • 22
    • 34547920745 scopus 로고    scopus 로고
    • An importin alpha/beta-recognized bipartite nuclear localization signal mediates targeting of the human herpes simplex virus type 1 DNA polymerase catalytic subunit pUL30 to the nucleus
    • Alvisi, G., Musiani, D., Jans, D. A., and Ripalti, A. (2007) An importin alpha/beta-recognized bipartite nuclear localization signal mediates targeting of the human herpes simplex virus type 1 DNA polymerase catalytic subunit pUL30 to the nucleus. Biochemistry 46, 9155-9163
    • (2007) Biochemistry , vol.46 , pp. 9155-9163
    • Alvisi, G.1    Musiani, D.2    Jans, D.A.3    Ripalti, A.4
  • 23
    • 33745631245 scopus 로고    scopus 로고
    • Quantitative analysis of localization and nuclear aggregate formation induced by GFP-lamin a mutant proteins in living HeLa cells
    • Hubner, S., Eam, J. E., Wagstaff, K. M., and Jans, D. A. (2006) Quantitative analysis of localization and nuclear aggregate formation induced by GFP-lamin A mutant proteins in living HeLa cells. J. Cell. Biochem. 98, 810-826
    • (2006) J. Cell. Biochem. , vol.98 , pp. 810-826
    • Hubner, S.1    Eam, J.E.2    Wagstaff, K.M.3    Jans, D.A.4
  • 24
    • 25444491192 scopus 로고    scopus 로고
    • Nuclear import of the respiratory syncytial virus matrix protein is mediated by importin beta1 independent of importin alpha
    • Ghildyal, R., Ho, A., Wagstaff, K. M., Dias, M. M., Barton, C. L., Jans, P., Bardin, P., and Jans, D. A. (2005) Nuclear import of the respiratory syncytial virus matrix protein is mediated by importin beta1 independent of importin alpha. Biochemistry 44, 12887-12895
    • (2005) Biochemistry , vol.44 , pp. 12887-12895
    • Ghildyal, R.1    Ho, A.2    Wagstaff, K.M.3    Dias, M.M.4    Barton, C.L.5    Jans, P.6    Bardin, P.7    Jans, D.A.8
  • 25
    • 0038136890 scopus 로고    scopus 로고
    • Role of prodomain in importin-mediated nuclear localization and activation of caspase-2
    • Baliga, B. C., Colussi, P. A., Read, S. H., Dias, M. M., Jans, D. A., and Kumar, S. (2003) Role of prodomain in importin-mediated nuclear localization and activation of caspase-2. J. Biol. Chem. 278, 4899-4905
    • (2003) J. Biol. Chem. , vol.278 , pp. 4899-4905
    • Baliga, B.C.1    Colussi, P.A.2    Read, S.H.3    Dias, M.M.4    Jans, D.A.5    Kumar, S.6
  • 26
    • 33744950505 scopus 로고    scopus 로고
    • Human cytomegalovirus (HCMV) DNA polymerase processivity factor ppUL44 dimerizes in the cytosol before translocation to the nucleus
    • Alvisi, G., Jans, D. A., and Ripalti, A. (2006) Human cytomegalovirus (HCMV) DNA polymerase processivity factor ppUL44 dimerizes in the cytosol before translocation to the nucleus. Biochemistry 45, 6866-6872
    • (2006) Biochemistry , vol.45 , pp. 6866-6872
    • Alvisi, G.1    Jans, D.A.2    Ripalti, A.3
  • 29
    • 23844445433 scopus 로고    scopus 로고
    • Apoptin nuclear accumulation is modulated by a CRM1-recognized nuclear export signal that is active in normal but not in tumor cells
    • Poon, I. K., Oro, C., Dias, M. M., Zhang, J., and Jans, D. A. (2005) Apoptin nuclear accumulation is modulated by a CRM1-recognized nuclear export signal that is active in normal but not in tumor cells. Cancer Res. 65, 7059-7064
    • (2005) Cancer Res. , vol.65 , pp. 7059-7064
    • Poon, I.K.1    Oro, C.2    Dias, M.M.3    Zhang, J.4    Jans, D.A.5
  • 30
    • 11144241881 scopus 로고    scopus 로고
    • A tumor cell-specific nuclear targeting signal within chicken anemia virus VP3/apoptin
    • Poon, I. K., Oro, C., Dias, M. M., Zhang, J. P., and Jans, D. A. (2005) A tumor cell-specific nuclear targeting signal within chicken anemia virus VP3/apoptin. J. Virol. 79, 1339-1341
    • (2005) J. Virol. , vol.79 , pp. 1339-1341
    • Poon, I.K.1    Oro, C.2    Dias, M.M.3    Zhang, J.P.4    Jans, D.A.5
  • 31
    • 0031847334 scopus 로고    scopus 로고
    • Perforin-dependent nuclear entry of granzyme B precedes apoptosis, and is not a consequence of nuclear membrane dysfunction
    • Trapani, J. A., Jans, P., Smyth, M. J., Froelich, C. J., Williams, E. A., Sutton, V. R., and Jans, D. A. (1998) Perforin-dependent nuclear entry of granzyme B precedes apoptosis, and is not a consequence of nuclear membrane dysfunction. Cell Death Differ. 5, 488-496 (Pubitemid 28356567)
    • (1998) Cell Death and Differentiation , vol.5 , Issue.6 , pp. 488-496
    • Trapani, J.A.1    Jans, P.2    Smyth, M.J.3    Froelich, C.J.4    Williams, E.A.5    Sutton, V.R.6    Jans, D.A.7
  • 32
    • 0032947291 scopus 로고    scopus 로고
    • The amino-terminal region of Vpr from human immunodeficiency virus type 1 forms ion channels and kills neurons
    • Piller, S. C., Ewart, G. D., Jans, D. A., Gage, P. W., and Cox, G. B. (1999) The amino-terminal region of Vpr from human immunodeficiency virus type 1 forms ion channels and kills neurons. J. Virol. 73, 4230-4238
    • (1999) J. Virol. , vol.73 , pp. 4230-4238
    • Piller, S.C.1    Ewart, G.D.2    Jans, D.A.3    Gage, P.W.4    Cox, G.B.5
  • 33
    • 0034932940 scopus 로고    scopus 로고
    • Nucleocytoplasmic distribution of the ovalbumin serpin PI-9 requires a nonconventional nuclear import pathway and the export factor Crm1
    • Bird, C. H., Blink, E. J., Hirst, C. E., Buzza, M. S., Steele, P. M., Sun, J., Jans, D. A., and Bird, P. I. (2001) Nucleocytoplasmic distribution of the ovalbumin serpin PI-9 requires a nonconventional nuclear import pathway and the export factor Crm1. Mol. Cell. Biol. 21, 5396-5407
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5396-5407
    • Bird, C.H.1    Blink, E.J.2    Hirst, C.E.3    Buzza, M.S.4    Steele, P.M.5    Sun, J.6    Jans, D.A.7    Bird, P.I.8
  • 34
    • 0029844220 scopus 로고    scopus 로고
    • Nuclear transport of granzyme B (Fragmentin-2) dependence on perforin in VIVO and cytosolic factors in vitro
    • Jans, D. A., Jans, P., Briggs, L. J., Sutton, V., and Trapani, J. A. (1996) Nuclear transport of granzyme B (fragmentin-2). Dependence of perforin in vivo and cytosolic factors in vitro. J. Biol. Chem. 271, 30781-30789 (Pubitemid 126751316)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.48 , pp. 30781-30789
    • Jans, D.A.1    Jans, P.2    Briggs, L.J.3    Sutton, V.4    Trapani, J.A.5
  • 35
    • 20544465655 scopus 로고    scopus 로고
    • FRAP analysis of nucleocytoplasmic dynamics of the vitamin D receptor splice variant VDRB1: Preferential targeting to nuclear speckles
    • Sunn, K. L., Eisman, J. A., Gardiner, E. M., and Jans, D. A. (2005) FRAP analysis of nucleocytoplasmic dynamics of the vitamin D receptor splice variant VDRB1: preferential targeting to nuclear speckles. Biochem. J. 388, 509-514
    • (2005) Biochem. J. , vol.388 , pp. 509-514
    • Sunn, K.L.1    Eisman, J.A.2    Gardiner, E.M.3    Jans, D.A.4
  • 36
    • 29144504314 scopus 로고    scopus 로고
    • Intramolecular masking of nuclear localization signals: Analysis of importin binding using a novel AlphaScreen-based method
    • Wagstaff, K. M., and Jans, D. A. (2006) Intramolecular masking of nuclear localization signals: analysis of importin binding using a novel AlphaScreen-based method. Anal. Biochem. 348, 49-56
    • (2006) Anal. Biochem. , vol.348 , pp. 49-56
    • Wagstaff, K.M.1    Jans, D.A.2
  • 37
    • 0025900402 scopus 로고
    • Nuclear localization of budgerigar fledgling disease virus capsid protein VP2 is conferred by residues 308-317
    • Rihs, H. P., Peters, R., and Hobom, G. (1991) Nuclear localization of budgerigar fledgling disease virus capsid protein VP2 is conferred by residues 308-317. FEBS Lett. 291, 6-8
    • (1991) FEBS Lett. , vol.291 , pp. 6-8
    • Rihs, H.P.1    Peters, R.2    Hobom, G.3
  • 38
    • 0032911885 scopus 로고    scopus 로고
    • The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals
    • Truant, R., and Cullen, B. R. (1999) The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals. Mol. Cell. Biol. 19, 1210-1217 (Pubitemid 29046863)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.2 , pp. 1210-1217
    • Truant, R.1    Cullen, B.R.2
  • 39
    • 0021352749 scopus 로고
    • DNA-binding activity of simian virus 40 large T antigen correlates with a distinct phosphorylation state
    • Scheidtmann, K. H., Hardung, M., Echle, B., and Walter, G. (1984) DNA-binding activity of simian virus 40 large T antigen correlates with a distinct phosphorylation state. J. Virol. 50, 1-12 (Pubitemid 14165284)
    • (1984) Journal of Virology , vol.50 , Issue.1 , pp. 1-12
    • Scheidtmann, K.H.1    Hardung, M.2    Echle, B.3    Walter, G.4
  • 42
    • 0030589598 scopus 로고    scopus 로고
    • Transportin: Nuclear transport receptor of a novel nuclear protein import pathway
    • Nakielny, S., Siomi, M. C., Siomi, H., Michael, W. M., Pollard, V., and Dreyfuss, G. (1996) Transportin: nuclear transport receptor of a novel nuclear protein import pathway. Exp. Cell. Res. 229, 261-266
    • (1996) Exp. Cell. Res. , vol.229 , pp. 261-266
    • Nakielny, S.1    Siomi, M.C.2    Siomi, H.3    Michael, W.M.4    Pollard, V.5    Dreyfuss, G.6
  • 43
    • 0030971249 scopus 로고    scopus 로고
    • Nuclear import of hnRNP A1 is mediated by a novel cellular cofactor related to karyopherin-beta
    • Fridell, R. A., Truant, R., Thorne, L., Benson, R. E., and Cullen, B. R. (1997) Nuclear import of hnRNP A1 is mediated by a novel cellular cofactor related to karyopherin-beta. J. Cell Sci. 110, 1325-1331 (Pubitemid 27273703)
    • (1997) Journal of Cell Science , vol.110 , Issue.11 , pp. 1325-1331
    • Fridell, R.A.1    Truant, R.2    Thorne, L.3    Benson, R.E.4    Cullen, B.R.5
  • 44
    • 0034823780 scopus 로고    scopus 로고
    • Regulation of p53 localization
    • Liang, S. H., and Clarke, M. F. (2001) Regulation of p53 localization. Eur. J. Biochem. 268, 2779-2783
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2779-2783
    • Liang, S.H.1    Clarke, M.F.2
  • 46
    • 0037032462 scopus 로고    scopus 로고
    • Identification of the nuclear localization signal of p21(cip1) and consequences of its mutation on cell proliferation
    • Rodriguez-Vilarrupla, A., Diaz, C., Canela, N., Rahn, H. P., Bachs, O., and Agell, N. (2002) Identification of the nuclear localization signal of p21(cip1) and consequences of its mutation on cell proliferation. FEBS Lett. 531, 319-323
    • (2002) FEBS Lett. , vol.531 , pp. 319-323
    • Rodriguez-Vilarrupla, A.1    Diaz, C.2    Canela, N.3    Rahn, H.P.4    Bachs, O.5    Agell, N.6
  • 47
    • 33745150087 scopus 로고    scopus 로고
    • The intricacies of p21 phosphorylation: Protein/protein interactions, subcellular localization and stability
    • Child, E. S., and Mann, D. J. (2006) The intricacies of p21 phosphorylation: protein/protein interactions, subcellular localization and stability. Cell Cycle 5, 1313-1319
    • (2006) Cell Cycle , vol.5 , pp. 1313-1319
    • Child, E.S.1    Mann, D.J.2
  • 48
    • 0242321145 scopus 로고    scopus 로고
    • BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential
    • Nakajima, A., Kataoka, K., Hong, M., Sakaguchi, M., and Huh, N. H. (2003) BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential. Cancer Lett. 201, 195-201
    • (2003) Cancer Lett. , vol.201 , pp. 195-201
    • Nakajima, A.1    Kataoka, K.2    Hong, M.3    Sakaguchi, M.4    Huh, N.H.5
  • 49
    • 22444445802 scopus 로고    scopus 로고
    • Defective calmodulin-mediated nuclear transport of the sex-determining region of the Y chromosome (SRY) in XY sex reversal
    • Sim, H., Rimmer, K., Kelly, S., Ludbrook, L. M., Clayton, A. H., and Harley, V. R. (2005) Defective calmodulin-mediated nuclear transport of the sex-determining region of the Y chromosome (SRY) in XY sex reversal. Mol. Endocrinol. 19, 1884-1892
    • (2005) Mol. Endocrinol. , vol.19 , pp. 1884-1892
    • Sim, H.1    Rimmer, K.2    Kelly, S.3    Ludbrook, L.M.4    Clayton, A.H.5    Harley, V.R.6
  • 50
    • 0035958975 scopus 로고    scopus 로고
    • Compound effects of point mutations causing campomelic dysplasia/autosomal sex reversal upon SOX9 structure, nuclear transport, DNA binding, and transcriptional activation
    • Preiss, S., Argentaro, A., Clayton, A., John, A., Jans, D. A., Ogata, T., Nagai, T., Barroso, I., Schafer, A. J., and Harley, V. R. (2001) Compound effects of point mutations causing campomelic dysplasia/autosomal sex reversal upon SOX9 structure, nuclear transport, DNA binding, and transcriptional activation. J. Biol. Chem. 276, 27864-27872
    • (2001) J. Biol. Chem. , vol.276 , pp. 27864-27872
    • Preiss, S.1    Argentaro, A.2    Clayton, A.3    John, A.4    Jans, D.A.5    Ogata, T.6    Nagai, T.7    Barroso, I.8    Schafer, A.J.9    Harley, V.R.10
  • 51
    • 0141445979 scopus 로고    scopus 로고
    • A SOX9 defect of calmodulin-dependent nuclear import in campomelic dysplasia/autosomal sex reversal
    • Argentaro, A., Sim, H., Kelly, S., Preiss, S., Clayton, A., Jans, D. A., and Harley, V. R. (2003) A SOX9 defect of calmodulin-dependent nuclear import in campomelic dysplasia/autosomal sex reversal. J. Biol. Chem. 278, 33839-33847
    • (2003) J. Biol. Chem. , vol.278 , pp. 33839-33847
    • Argentaro, A.1    Sim, H.2    Kelly, S.3    Preiss, S.4    Clayton, A.5    Jans, D.A.6    Harley, V.R.7
  • 52
    • 39549091696 scopus 로고    scopus 로고
    • Transcription factor NF-κB is transported to the nucleus via cytoplasmic dynein/dynactin motor complex in hippocampal neurons
    • Mikenberg, I., Widera, D., Kaus, A., Kaltschmidt, B., and Kaltschmidt, C. (2007) Transcription factor NF-κB is transported to the nucleus via cytoplasmic dynein/dynactin motor complex in hippocampal neurons. PLoS ONE 2, e589
    • (2007) PLoS ONE , vol.2
    • Mikenberg, I.1    Widera, D.2    Kaus, A.3    Kaltschmidt, B.4    Kaltschmidt, C.5
  • 53
    • 43949097898 scopus 로고    scopus 로고
    • Nuclear localization sequences in cytomegalovirus capsid assembly proteins (UL80 proteins) are required for virus production: Inactivating NLS1, NLS2, or both affects replication to strikingly different extents
    • Nguyen, N. L., Loveland, A. N., and Gibson, W. (2008) Nuclear localization sequences in cytomegalovirus capsid assembly proteins (UL80 proteins) are required for virus production: inactivating NLS1, NLS2, or both affects replication to strikingly different extents. J. Virol. 82, 5381-5389
    • (2008) J. Virol. , vol.82 , pp. 5381-5389
    • Nguyen, N.L.1    Loveland, A.N.2    Gibson, W.3
  • 54
    • 44349146579 scopus 로고    scopus 로고
    • Functional mapping of the porcine reproductive and respiratory syndrome virus capsid protein nuclear localization signal and its pathogenic association
    • Pei, Y., Hodgins, D. C., Lee, C., Calvert, J. G., Welch, S. K., Jolie, R., Keith, M., and Yoo, D. (2008) Functional mapping of the porcine reproductive and respiratory syndrome virus capsid protein nuclear localization signal and its pathogenic association. Virus Res. 135, 107-114
    • (2008) Virus Res. , vol.135 , pp. 107-114
    • Pei, Y.1    Hodgins, D.C.2    Lee, C.3    Calvert, J.G.4    Welch, S.K.5    Jolie, R.6    Keith, M.7    Yoo, D.8
  • 55
    • 66149117071 scopus 로고    scopus 로고
    • The respiratory syncytial virus matrix protein possesses a Crm1-mediated nuclear export mechanism
    • Ghildyal, R., Ho, A., Dias, M., Soegiyono, L., Bardin, P. G., Tran, K. C., Teng, M. N., and Jans, D. A. (2009) The respiratory syncytial virus matrix protein possesses a Crm1-mediated nuclear export mechanism. J. Virol. 83, 5353-5362
    • (2009) J. Virol. , vol.83 , pp. 5353-5362
    • Ghildyal, R.1    Ho, A.2    Dias, M.3    Soegiyono, L.4    Bardin, P.G.5    Tran, K.C.6    Teng, M.N.7    Jans, D.A.8
  • 56
    • 34250899898 scopus 로고    scopus 로고
    • Nuclear localization of dengue virus nonstructural protein 5 through its importin alpha/beta-recognized nuclear localization sequences is integral to viral infection
    • Pryor, M. J., Rawlinson, S. M., Butcher, R. E., Barton, C. L., Waterhouse, T. A., Vasudevan, S. G., Bardin, P. G., Wright, P. J., Jans, D. A., and Davidson, A. D. (2007) Nuclear localization of dengue virus nonstructural protein 5 through its importin alpha/beta-recognized nuclear localization sequences is integral to viral infection. Traffic 8, 795-807
    • (2007) Traffic , vol.8 , pp. 795-807
    • Pryor, M.J.1    Rawlinson, S.M.2    Butcher, R.E.3    Barton, C.L.4    Waterhouse, T.A.5    Vasudevan, S.G.6    Bardin, P.G.7    Wright, P.J.8    Jans, D.A.9    Davidson, A.D.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.