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Volumn 120, Issue 2, 2007, Pages 265-275

A B23-interacting sequence as a tool to visualize protein interactions in a cellular context

Author keywords

NoLS; Nucleolus; Protein B23; Protein interaction; Targeting

Indexed keywords

FIBRILLARIN; GREEN FLUORESCENT PROTEIN; NUCLEOPHOSMIN; PROTEIN NOP56; REV PROTEIN; SMALL NUCLEOLAR RIBONUCLEOPROTEIN; TRANSCRIPTION FACTOR MAFG; TRANSCRIPTION FACTOR NF E2; UNCLASSIFIED DRUG;

EID: 33846976164     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.03345     Document Type: Article
Times cited : (35)

References (46)
  • 1
    • 0027252951 scopus 로고
    • Nucleolar targeting signal of Rex protein of human T-cell leukemia virus type I specifically binds to nucleolar shuttle protein B-23
    • Adachi, Y., Copeland, T. D., Hatanaka, M. and Oroszlan, S. (1993). Nucleolar targeting signal of Rex protein of human T-cell leukemia virus type I specifically binds to nucleolar shuttle protein B-23. J. Biol. Chem. 268, 13930-13934.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13930-13934
    • Adachi, Y.1    Copeland, T.D.2    Hatanaka, M.3    Oroszlan, S.4
  • 2
    • 0024966024 scopus 로고
    • Major nucleolar proteins shuttle between nucleus and cytoplasm
    • Borer, R. A., Lehner, C. F., Eppenberger, H. M. and Nigg, E. A. (1989). Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 56, 379-390.
    • (1989) Cell , vol.56 , pp. 379-390
    • Borer, R.A.1    Lehner, C.F.2    Eppenberger, H.M.3    Nigg, E.A.4
  • 3
    • 0035795422 scopus 로고    scopus 로고
    • Nucleolar components involved in ribosome biogenesis cycle between the nucleolus and nucleoplasm in interphase cells
    • Chen, D. and Huang, S. (2001). Nucleolar components involved in ribosome biogenesis cycle between the nucleolus and nucleoplasm in interphase cells. J. Cell Biol. 153, 169-176.
    • (2001) J. Cell Biol. , vol.153 , pp. 169-176
    • Chen, D.1    Huang, S.2
  • 4
    • 0024431720 scopus 로고
    • Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins
    • Dang, C. V. and Lee, W. M. F. (1989). Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins. J. Biol. Chem. 264, 18019-18023.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18019-18023
    • Dang, C.V.1    Lee, W.M.F.2
  • 7
    • 33645802652 scopus 로고    scopus 로고
    • Both carboxy-terminus NES motif and mutated tryptophan(s) are crucial for aberrant nuclear export of nucleophosmin leukemic mutants in NPMc+ AML
    • Falini, B., Bolli, N., Shan, J., Martelli, M. P., Liso, A., Pucciarini, A., Bigerna, B., Pasqualucci, L., Mannucci, R., Rosati, R. et al. (2006). Both carboxy-terminus NES motif and mutated tryptophan(s) are crucial for aberrant nuclear export of nucleophosmin leukemic mutants in NPMc+ AML. Blood 107, 4514-4523.
    • (2006) Blood , vol.107 , pp. 4514-4523
    • Falini, B.1    Bolli, N.2    Shan, J.3    Martelli, M.P.4    Liso, A.5    Pucciarini, A.6    Bigerna, B.7    Pasqualucci, L.8    Mannucci, R.9    Rosati, R.10
  • 8
    • 0026352122 scopus 로고
    • Specific complex of human immunodeficiency virus type I rev and nucleolar B23 proteins: Dissociation by the Rev response element
    • Fankhauser, C., Izaurralde, E., Adachi, Y., Wingfield, P. and Laemmli, U. K. (1991). Specific complex of human immunodeficiency virus type I rev and nucleolar B23 proteins: dissociation by the Rev response element. Mol. Cell. Biol. 11, 2567-2575.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2567-2575
    • Fankhauser, C.1    Izaurralde, E.2    Adachi, Y.3    Wingfield, P.4    Laemmli, U.K.5
  • 10
    • 14644412785 scopus 로고    scopus 로고
    • Nucleolus: An essential nuclear domain
    • In (ed. P. Hemmerich and S. Dickmann), Los Angeles, CA: American Scientific Publishers
    • Gébrane-Younès, J., Sirri, V., Junéra, H. R., Roussel, P. and Hernandez-Verdun, D. (2005). Nucleolus: an essential nuclear domain. In Visions of the Cell Nucleus (ed. P. Hemmerich and S. Dickmann), pp. 120-135. Los Angeles, CA: American Scientific Publishers.
    • (2005) Visions of the Cell Nucleus , pp. 120-135
    • Gébrane-Younès, J.1    Sirri, V.2    Junéra, H.R.3    Roussel, P.4    Hernandez-Verdun, D.5
  • 13
    • 30044434446 scopus 로고    scopus 로고
    • Nucleolus: From structure to dynamics
    • Hernandez-Verdun, D. (2006). Nucleolus: from structure to dynamics. Histochem. Cell Biol. 125, 127-137.
    • (2006) Histochem. Cell Biol. , vol.125 , pp. 127-137
    • Hernandez-Verdun, D.1
  • 14
    • 0029914227 scopus 로고    scopus 로고
    • Sedimentation analyses of the salt- and divalent metal ion-induced oligomerization of nocleolar protein B23
    • Herrera, J. E., Correia, J. J., Jones, A. E. and Olson, M. O. J. (1996). Sedimentation analyses of the salt- and divalent metal ion-induced oligomerization of nocleolar protein B23. Biochemistry 35, 2668-2673.
    • (1996) Biochemistry , vol.35 , pp. 2668-2673
    • Herrera, J.E.1    Correia, J.J.2    Jones, A.E.3    Olson, M.O.J.4
  • 15
    • 0034637578 scopus 로고    scopus 로고
    • Mapping the functional domains of nucleolar protein B23
    • Hingorani, K., Szebeni, A. and Olson, M. O. J. (2000). Mapping the functional domains of nucleolar protein B23. J. Biol. Chem. 275, 24451-24457.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24451-24457
    • Hingorani, K.1    Szebeni, A.2    Olson, M.O.J.3
  • 16
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C. D., Chinenov, Y. and Kerppolla, T. K. (2002). Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9, 789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppolla, T.K.3
  • 17
    • 14044259319 scopus 로고    scopus 로고
    • Protein NPM3 interacts with the multifunctional nucleolar protein B23 /NPM and inhibits ribosome biogenesis
    • Huang, N., Negi, S., Szebeni, A. and Olson, M. O. J. (2005). Protein NPM3 interacts with the multifunctional nucleolar protein B23/NPM and inhibits ribosome biogenesis. J. Biol. Chem. 280, 5496-5502.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5496-5502
    • Huang, N.1    Negi, S.2    Szebeni, A.3    Olson, M.O.J.4
  • 18
    • 0345276485 scopus 로고    scopus 로고
    • Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation
    • Itahana, K., Bhat, K. P., Jin, A., Itahana, Y., Hawke, D., Kobayashi, R. and Zhang, Y. (2003). Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation. Mol. Cell 12, 1151-1164.
    • (2003) Mol. Cell , vol.12 , pp. 1151-1164
    • Itahana, K.1    Bhat, K.P.2    Jin, A.3    Itahana, Y.4    Hawke, D.5    Kobayashi, R.6    Zhang, Y.7
  • 20
    • 0024325692 scopus 로고
    • Functional similarity of HIV-I rev and HTLV-I rex proteins: Identification of a new nucleolar-targeting signal in rev protein
    • Kubota, S., Siomi, H., Satoh, T., Endo, S., Maki, M. and Hatanaka, M. (1989). Functional similarity of HIV-I rev and HTLV-I rex proteins: identification of a new nucleolar-targeting signal in rev protein. Biochem. Biophys. Res. Commun. 162, 963-970.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 963-970
    • Kubota, S.1    Siomi, H.2    Satoh, T.3    Endo, S.4    Maki, M.5    Hatanaka, M.6
  • 21
    • 0030956564 scopus 로고    scopus 로고
    • Protein B23 is an important human factor for the nucleolar localization of the human immunodeficiency virus protein Tat
    • Li, Y. P. (1997). Protein B23 is an important human factor for the nucleolar localization of the human immunodeficiency virus protein Tat. J. Virol. 71, 4098-4102.
    • (1997) J. Virol. , vol.71 , pp. 4098-4102
    • Li, Y.P.1
  • 22
    • 0029962298 scopus 로고    scopus 로고
    • C23 interacts with B23, a putative nucleolar-localization-signal-binding protein
    • Li, Y. P., Busch, R. K., Valdez, B. C. and Busch, H. (1996). C23 interacts with B23, a putative nucleolar-localization-signal-binding protein. Eur. J. Biochem. 237, 153-158.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 153-158
    • Li, Y.P.1    Busch, R.K.2    Valdez, B.C.3    Busch, H.4
  • 23
    • 0033179146 scopus 로고    scopus 로고
    • Nuclear bodies: Multifaceted subdomains of the interchromatin space
    • Matera, A. G. (1999). Nuclear bodies: multifaceted subdomains of the interchromatin space. Trends Cell Biol. 9, 302-309.
    • (1999) Trends Cell Biol. , vol.9 , pp. 302-309
    • Matera, A.G.1
  • 24
    • 0029055194 scopus 로고
    • The nucleolus: An organelle formed by the act of building a ribosome
    • Mélèse, T. and Xue, Z. (1995). The nucleolus: an organelle formed by the act of building a ribosome. Curr. Opin. Cell Biol. 7, 319-324.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 319-324
    • Mélèse, T.1    Xue, Z.2
  • 25
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli, T. (2001). Protein dynamics: implications for nuclear architecture and gene expression. Science 291, 843-847.
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 26
    • 0035985191 scopus 로고    scopus 로고
    • The RNA binding activity of a ribosome biogenesis factor, nucleophosmin /B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype
    • Okuwaki, M., Tsujimoto, M. and Nagata, K. (2002). The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype. Mol. Biol. Cell 13, 2016-2030.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2016-2030
    • Okuwaki, M.1    Tsujimoto, M.2    Nagata, K.3
  • 27
    • 18244366700 scopus 로고    scopus 로고
    • Nontraditional roles of the nucleolus
    • In (ed. M. O. J. Olson), Georgetown, TX: Landes Bioscience
    • Olson, M. O. J. (2004). Nontraditional roles of the nucleolus. In The Nucleolus (ed. M. O. J. Olson), pp. 329-342. Georgetown, TX: Landes Bioscience.
    • (2004) The Nucleolus , pp. 329-342
    • Olson, M.O.J.1
  • 28
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R. D. and Misteli, T. (2000). High mobility of proteins in the mammalian cell nucleus. Nature 404, 604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 29
    • 0032796373 scopus 로고    scopus 로고
    • The nucleolar antigen Nop52, the human homologue of the yeast ribosomal RNA processing RRP1, is recruited at late stages of nucleologenesis
    • Savino, T. M., Bastos, R., Jansen, E. and Hernandez-Verdun, D. (1999). The nucleolar antigen Nop52, the human homologue of the yeast ribosomal RNA processing RRP1, is recruited at late stages of nucleologenesis. J. Cell Sci. 112, 1889-1900.
    • (1999) J. Cell Sci. , vol.112 , pp. 1889-1900
    • Savino, T.M.1    Bastos, R.2    Jansen, E.3    Hernandez-Verdun, D.4
  • 30
    • 0032189707 scopus 로고    scopus 로고
    • Preferential cleavage in pre-ribosomal RNA by protein B23 endoribonuclease
    • Savkur, R. S. and Olson, M. O. J. (1998). Preferential cleavage in pre-ribosomal RNA by protein B23 endoribonuclease. Nucleic Acids Res. 26, 4508-4515.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4508-4515
    • Savkur, R.S.1    Olson, M.O.J.2
  • 31
    • 0033153298 scopus 로고    scopus 로고
    • Structure and function of the nucleolus
    • Scheer, U. and Hock, R. (1999). Structure and function of the nucleolus. Curr. Opin. Cell Biol. 11, 385-390.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 385-390
    • Scheer, U.1    Hock, R.2
  • 32
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin, P. R. (2000). The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 7, 730-734.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 34
    • 0023812595 scopus 로고
    • Sequence requirements for nucleolar localization of human T cell leukemia virus type I pX protein, which regulates viral RNA processing
    • Siomi, H., Shida, H., Nam, S. H., Nosaka, T., Maki, M. and Hatanaka, M. (1988). Sequence requirements for nucleolar localization of human T cell leukemia virus type I pX protein, which regulates viral RNA processing. Cell 55, 197-209.
    • (1988) Cell , vol.55 , pp. 197-209
    • Siomi, H.1    Shida, H.2    Nam, S.H.3    Nosaka, T.4    Maki, M.5    Hatanaka, M.6
  • 35
    • 0037128933 scopus 로고    scopus 로고
    • Cyclin-dependent kinases govern formation and maintenance of the nucleolus
    • Sirri, V., Hernandez-Verdun, D. and Roussel, P. (2002). Cyclin-dependent kinases govern formation and maintenance of the nucleolus. J. Cell Biol. 156, 969-981.
    • (2002) J. Cell Biol. , vol.156 , pp. 969-981
    • Sirri, V.1    Hernandez-Verdun, D.2    Roussel, P.3
  • 36
    • 0034735515 scopus 로고    scopus 로고
    • Mutational analysis of fibrillarin and its mobility in living human cells
    • Snaar, S., Wiesmeijer, K., Jochemsen, A. G., Tanke, H. J. and Dirks, R. W. (2000). Mutational analysis of fibrillarin and its mobility in living human cells. J. Cell Biol. 151, 653-662.
    • (2000) J. Cell Biol. , vol.151 , pp. 653-662
    • Snaar, S.1    Wiesmeijer, K.2    Jochemsen, A.G.3    Tanke, H.J.4    Dirks, R.W.5
  • 37
    • 17844396708 scopus 로고    scopus 로고
    • Identification of a novel nucleolar localization signal and a degradation signal in Survivin-deltaEx3: A potential link between nucleolus and protein degradation
    • Song, Z. and Wu, M. (2005). Identification of a novel nucleolar localization signal and a degradation signal in Survivin-deltaEx3: a potential link between nucleolus and protein degradation. Oncogene 24, 2723-2734.
    • (2005) Oncogene , vol.24 , pp. 2723-2734
    • Song, Z.1    Wu, M.2
  • 38
    • 0034851781 scopus 로고    scopus 로고
    • Nuclear domains
    • Spector, D. L. (2001). Nuclear domains. J. Cell Sci. 114, 2891-2893.
    • (2001) J. Cell Sci. , vol.114 , pp. 2891-2893
    • Spector, D.L.1
  • 39
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: Proper and fitting
    • Sprague, B. L. and McNally, J. G. (2005). FRAP analysis of binding: proper and fitting. Trends Cell Biol. 15, 84-91.
    • (2005) Trends Cell Biol. , vol.15 , pp. 84-91
    • Sprague, B.L.1    McNally, J.G.2
  • 40
    • 0029791261 scopus 로고    scopus 로고
    • Functional compartmentalization of the nucleus
    • Strouboulis, J. and Wolffe, A. P. (1996). Functional compartmentalization of the nucleus. J. Cell Sci. 109, 1991-2000.
    • (1996) J. Cell Sci. , vol.109 , pp. 1991-2000
    • Strouboulis, J.1    Wolffe, A.P.2
  • 41
    • 0037646535 scopus 로고    scopus 로고
    • Role of protein kinase CK2 phosphorylation in the molecular chaperone activity of nucleolar protein B23
    • Szebeni, A., Hingorani, K., Negi, S. and Olson, M. O. J. (2003). Role of protein kinase CK2 phosphorylation in the molecular chaperone activity of nucleolar protein B23. J. Biol. Chem. 278, 9107-9115.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9107-9115
    • Szebeni, A.1    Hingorani, K.2    Negi, S.3    Olson, M.O.J.4
  • 43
    • 0028122251 scopus 로고
    • Identification of the nuclear and nucleolar localization signals of the protein p120. Interaction with translocation protein B23
    • Valdez, B. C., Perlaky, L., Henning, D., Saijo, Y., Chan, P. K. and Busch, H. (1994). Identification of the nuclear and nucleolar localization signals of the protein p120. Interaction with translocation protein B23. J. Biol. Chem. 269, 23776-23783.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23776-23783
    • Valdez, B.C.1    Perlaky, L.2    Henning, D.3    Saijo, Y.4    Chan, P.K.5    Busch, H.6
  • 46
    • 0034001337 scopus 로고    scopus 로고
    • Conserved composition of mammalian box H/ACA and box C/D small nucleolar ribonucleoprotein particles and their interaction with the common factor Nopp140
    • Yang, Y., Isaac, C., Wang, C., Dragon, F., Pogacic, V. and Meier, U. T. (2000). Conserved composition of mammalian box H/ACA and box C/D small nucleolar ribonucleoprotein particles and their interaction with the common factor Nopp140. Mol. Biol. Cell 11, 567-577.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 567-577
    • Yang, Y.1    Isaac, C.2    Wang, C.3    Dragon, F.4    Pogacic, V.5    Meier, U.T.6


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