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Volumn 4, Issue 7, 2009, Pages

Structure-function analysis of nucleolin and ErbB receptors interactions

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; NUCLEOLIN; EGFR PROTEIN, HUMAN; PHOSPHOPROTEIN; PRIMER DNA; RNA BINDING PROTEIN;

EID: 67650337250     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0006128     Document Type: Article
Times cited : (27)

References (48)
  • 1
    • 0021273420 scopus 로고
    • Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
    • Ullrich A, Coussens L, Hayflick JS, Dull TJ, Gray A, et al. (1984) Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature 309: 418-425.
    • (1984) Nature , vol.309 , pp. 418-425
    • Ullrich, A.1    Coussens, L.2    Hayflick, J.S.3    Dull, T.J.4    Gray, A.5
  • 2
    • 0022399581 scopus 로고
    • Tyrosine kinase receptor with extensive homology to EGF receptor shares chromosomal location with neu oncogene
    • Coussens L, Yang Feng Tl, Liao YC, Chen E, Gray A, et al. (1985) Tyrosine kinase receptor with extensive homology to EGF receptor shares chromosomal location with neu oncogene. Science 230: 1132-1139.
    • (1985) Science , vol.230 , pp. 1132-1139
    • Coussens, L.1    Yang Feng, T.2    Liao, Y.C.3    Chen, E.4    Gray, A.5
  • 3
    • 0022600388 scopus 로고
    • The neu oncogene encodes an epidermal growth factor receptor-related protein
    • Bargmann CI, Hung MC, Weinberg RA (1986) The neu oncogene encodes an epidermal growth factor receptor-related protein. Nature 319: 226-230.
    • (1986) Nature , vol.319 , pp. 226-230
    • Bargmann, C.I.1    Hung, M.C.2    Weinberg, R.A.3
  • 4
    • 0022588467 scopus 로고
    • Similarity of protein encoded by the human c-erbB-2 gene to epidermal growth factor receptor
    • Yamamoto T, Ikawa S, Akiyama T, Semba K, Nomura N, et al. (1986) Similarity of protein encoded by the human c-erbB-2 gene to epidermal growth factor receptor. Nature 319: 230-234.
    • (1986) Nature , vol.319 , pp. 230-234
    • Yamamoto, T.1    Ikawa, S.2    Akiyama, T.3    Semba, K.4    Nomura, N.5
  • 5
    • 0025287954 scopus 로고
    • Molecular cloning and expression of an additional epidermal growth factor receptor-related gene
    • Plowman GD, Whitney GS, Neubauer MG, Green JM, McDonald VI, et al. (1990) Molecular cloning and expression of an additional epidermal growth factor receptor-related gene. Proc Natl Acad Sci USA 87: 4905-4909.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4905-4909
    • Plowman, G.D.1    Whitney, G.S.2    Neubauer, M.G.3    Green, J.M.4    McDonald, V.I.5
  • 6
    • 0024326947 scopus 로고
    • Isolation and characterization of ErbB-3, a third member of the ErbB/ epidermal growth factor receptor family: Evidence for overexpression in a subset of human mammary tumors
    • Kraus MH, Issing M, Popescu NC, Aaronson SA (1989) Isolation and characterization of ErbB-3, a third member of the ErbB/ epidermal growth factor receptor family: Evidence for overexpression in a subset of human mammary tumors. Proc Natl Acad Sci USA 86: 9193-9197.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9193-9197
    • Kraus, M.H.1    Issing, M.2    Popescu, N.C.3    Aaronson, S.A.4
  • 8
    • 3442890204 scopus 로고    scopus 로고
    • Role of HER receptors family in development and differentiation
    • Casalini P, Iorio MV, Galmozzi E, Menard S (2004) Role of HER receptors family in development and differentiation. J Cell Physiol 200: 343-350.
    • (2004) J Cell Physiol , vol.200 , pp. 343-350
    • Casalini, P.1    Iorio, M.V.2    Galmozzi, E.3    Menard, S.4
  • 10
    • 2142843806 scopus 로고    scopus 로고
    • Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions
    • Pinkas-Kramarski R, Soussan L, Waterman H, Levkowitz G, Alroy I, et al. (1996) Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions. The EMBO Journal 15: 2452-2467.
    • (1996) The EMBO Journal , vol.15 , pp. 2452-2467
    • Pinkas-Kramarski, R.1    Soussan, L.2    Waterman, H.3    Levkowitz, G.4    Alroy, I.5
  • 11
    • 0025765803 scopus 로고
    • SH-2 and SH-3 domains: Elements that control interactions of cytoplasmic signaling proteins
    • Koch AC, Anderson D, Moran MF, Ellis C, Pawson T (1991) SH-2 and SH-3 domains: Elements that control interactions of cytoplasmic signaling proteins. Science 252: 668-674.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, A.C.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 12
    • 0029067403 scopus 로고
    • PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine
    • Kavanaugh WM, Turck CW, Williams LT (1995) PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 268: 1177-1179.
    • (1995) Science , vol.268 , pp. 1177-1179
    • Kavanaugh, W.M.1    Turck, C.W.2    Williams, L.T.3
  • 13
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J (2000) Cell signaling by receptor tyrosine kinases. Cell 103: 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 15
    • 12144266330 scopus 로고    scopus 로고
    • Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation
    • Citri A, Gan J, Mosesson Y, Vereb G, Szollosi J, et al. (2004) Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation. EMBO Rep 5: 1165-1170.
    • (2004) EMBO Rep , vol.5 , pp. 1165-1170
    • Citri, A.1    Gan, J.2    Mosesson, Y.3    Vereb, G.4    Szollosi, J.5
  • 16
    • 0032754311 scopus 로고    scopus 로고
    • Molecular dissection of nucleolin's role in growth and cell proliferation: New insights
    • Srivastava M, Pollard HB (1999) Molecular dissection of nucleolin's role in growth and cell proliferation: new insights. FASEB J 13: 1911-1922.
    • (1999) FASEB J , vol.13 , pp. 1911-1922
    • Srivastava, M.1    Pollard, H.B.2
  • 18
    • 0020446437 scopus 로고
    • Detection and localization of a class of proteins immunologically related to a 100-kDa nucleolar protein
    • Bugler B, Caizergues-Ferrer M, Bouche G, Bourbon H, Amalric F (1982) Detection and localization of a class of proteins immunologically related to a 100-kDa nucleolar protein. Eur J Biochem 128: 475-480.
    • (1982) Eur J Biochem , vol.128 , pp. 475-480
    • Bugler, B.1    Caizergues-Ferrer, M.2    Bouche, G.3    Bourbon, H.4    Amalric, F.5
  • 19
    • 0027194488 scopus 로고
    • The self-cleaving activity of nucleolin determines its molecular dynamics in relation to cell proliferation
    • Fang SH, Yeh NH (1993) The self-cleaving activity of nucleolin determines its molecular dynamics in relation to cell proliferation. Exp Cell Res 208: 48-53.
    • (1993) Exp Cell Res , vol.208 , pp. 48-53
    • Fang, S.H.1    Yeh, N.H.2
  • 21
    • 34548779160 scopus 로고    scopus 로고
    • Inactivation of nucleolin leads to nucleolar disruption, cell cycle arrest and defects in centrosome duplication
    • Ugrinova I, Monier K, Ivaldi C, Thiry M, Storck S, et al. (2007) Inactivation of nucleolin leads to nucleolar disruption, cell cycle arrest and defects in centrosome duplication. BMC Mol Biol 8: 66.
    • (2007) BMC Mol Biol , vol.8 , pp. 66
    • Ugrinova, I.1    Monier, K.2    Ivaldi, C.3    Thiry, M.4    Storck, S.5
  • 22
    • 9144245356 scopus 로고    scopus 로고
    • Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cells
    • Legrand D, Vigie K, Said E, Elass E, Masson M, et al. (2004) Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cells. Eur J Biochem 271: 303-317.
    • (2004) Eur J Biochem , vol.271 , pp. 303-317
    • Legrand, D.1    Vigie, K.2    Said, E.3    Elass, E.4    Masson, M.5
  • 23
    • 47249109051 scopus 로고    scopus 로고
    • Nuclear translocation of urokinase-type plasminogen activator
    • Stepanova V, Lebedeva T, Kuo A, Yarovoi S, Tkachuk S, et al. (2008) Nuclear translocation of urokinase-type plasminogen activator. Blood 112: 100-110.
    • (2008) Blood , vol.112 , pp. 100-110
    • Stepanova, V.1    Lebedeva, T.2    Kuo, A.3    Yarovoi, S.4    Tkachuk, S.5
  • 25
    • 0033543548 scopus 로고    scopus 로고
    • Antiproliferative activity of G-rich oligonucleotides correlates with protein binding
    • Bates PJ, Kahlon JB, Thomas SD, Trent JO, Miller DM (1999) Antiproliferative activity of G-rich oligonucleotides correlates with protein binding. J Biol Chem 274: 26369-26377.
    • (1999) J Biol Chem , vol.274 , pp. 26369-26377
    • Bates, P.J.1    Kahlon, J.B.2    Thomas, S.D.3    Trent, J.O.4    Miller, D.M.5
  • 26
    • 35948945681 scopus 로고    scopus 로고
    • AS1411 alters the localization of a complex containing protein arginine methyltransferase 5 and nucleolin
    • Teng Y, Girvan AC, Casson LK, Pierce WM Jr, Qian M, et al. (2007) AS1411 alters the localization of a complex containing protein arginine methyltransferase 5 and nucleolin. Cancer Res 67: 10491-10500.
    • (2007) Cancer Res , vol.67 , pp. 10491-10500
    • Teng, Y.1    Girvan, A.C.2    Casson, L.K.3    Pierce Jr, W.M.4    Qian, M.5
  • 27
    • 0035900673 scopus 로고    scopus 로고
    • Inhibition of DNA replication and induction of S phase cell cycle arrest by G-rich oligonucleotides
    • Xu X, Hamhouyia F, Thomas SD, Burke TJ, Girvan AC, et al. (2001) Inhibition of DNA replication and induction of S phase cell cycle arrest by G-rich oligonucleotides. J Biol Chem 276: 43221-43230.
    • (2001) J Biol Chem , vol.276 , pp. 43221-43230
    • Xu, X.1    Hamhouyia, F.2    Thomas, S.D.3    Burke, T.J.4    Girvan, A.C.5
  • 29
    • 0032921853 scopus 로고    scopus 로고
    • Structure and functions of nucleolin
    • Ginisty H, Sicard H, Roger B, Bouvet P (1999) Structure and functions of nucleolin. J Cell Sci 112(Pt6): 761-772.
    • (1999) J Cell Sci , vol.112 , Issue.PT6 , pp. 761-772
    • Ginisty, H.1    Sicard, H.2    Roger, B.3    Bouvet, P.4
  • 30
    • 0032563213 scopus 로고    scopus 로고
    • Nucleolin interacts with several ribosomal proteins through its RGG domain
    • Bouvet P, Diaz JJ, Kindbeiter K, Madjar JJ, Amalric F (1998) Nucleolin interacts with several ribosomal proteins through its RGG domain. J Biol Chem 273: 19025-19029.
    • (1998) J Biol Chem , vol.273 , pp. 19025-19029
    • Bouvet, P.1    Diaz, J.J.2    Kindbeiter, K.3    Madjar, J.J.4    Amalric, F.5
  • 31
    • 33846681638 scopus 로고    scopus 로고
    • Nucleolin: A multiFACeTed protein
    • Mongelard F, Bouvet P (2007) Nucleolin: a multiFACeTed protein. Trends Cell Biol 17: 80-86.
    • (2007) Trends Cell Biol , vol.17 , pp. 80-86
    • Mongelard, F.1    Bouvet, P.2
  • 32
    • 8344279508 scopus 로고    scopus 로고
    • A basic peptide within the juxtamembrane region is required for EGF receptor dimerization
    • Aifa S, Aydin J, Nordvall G, Lundstrom I, Svensson SP, et al. (2005) A basic peptide within the juxtamembrane region is required for EGF receptor dimerization. Exp Cell Res 302: 108-114.
    • (2005) Exp Cell Res , vol.302 , pp. 108-114
    • Aifa, S.1    Aydin, J.2    Nordvall, G.3    Lundstrom, I.4    Svensson, S.P.5
  • 33
    • 34249845380 scopus 로고    scopus 로고
    • Characterization of a novel tripartite nuclear localization sequence in the EGFR family
    • Hsu SC, Hung MC (2007) Characterization of a novel tripartite nuclear localization sequence in the EGFR family. J Biol Chem 282: 10432-10440.
    • (2007) J Biol Chem , vol.282 , pp. 10432-10440
    • Hsu, S.C.1    Hung, M.C.2
  • 34
    • 33947118714 scopus 로고    scopus 로고
    • Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression
    • Liao HJ, Carpenter G (2007) Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression. Mol Biol Cell 18: 1064-1072.
    • (2007) Mol Biol Cell , vol.18 , pp. 1064-1072
    • Liao, H.J.1    Carpenter, G.2
  • 35
    • 0023942517 scopus 로고
    • Growth factor receptor tyrosine kinases
    • Yarden Y, Ullrich A (1988) Growth factor receptor tyrosine kinases. Ann Rev Biochem 57: 443-478.
    • (1988) Ann Rev Biochem , vol.57 , pp. 443-478
    • Yarden, Y.1    Ullrich, A.2
  • 36
    • 33646391491 scopus 로고    scopus 로고
    • The angiogenic function of nucleolin is mediated by vascular endothelial growth factor and nonmuscle myosin
    • Huang Y, Shi H, Zhou H, Song X, Yuan S, et al. (2006) The angiogenic function of nucleolin is mediated by vascular endothelial growth factor and nonmuscle myosin. Blood 107: 3564-3571.
    • (2006) Blood , vol.107 , pp. 3564-3571
    • Huang, Y.1    Shi, H.2    Zhou, H.3    Song, X.4    Yuan, S.5
  • 37
    • 28544448741 scopus 로고    scopus 로고
    • Endosomal transport of ErbB-2: Mechanism for nuclear entry of the cell surface receptor
    • Giri DK, Ali-Seyed M, Li LY, Lee DF, Ling P, et al. (2005) Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. Mol Cell Biol 25: 11005-11018.
    • (2005) Mol Cell Biol , vol.25 , pp. 11005-11018
    • Giri, D.K.1    Ali-Seyed, M.2    Li, L.Y.3    Lee, D.F.4    Ling, P.5
  • 38
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • Ferguson KM, Berger MB, Mendrola JM, Cho HS, Leahy DJ, et al. (2003) EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell 11: 507-517.
    • (2003) Mol Cell , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5
  • 39
    • 0034468319 scopus 로고    scopus 로고
    • The carboxy-terminal fragment of nucleolin interacts with the nucleocapsid domain of retroviral gag proteins and inhibits virion assembly
    • Bacharach E, Gonsky J, Alin K, Orlova M, Goff SP (2000) The carboxy-terminal fragment of nucleolin interacts with the nucleocapsid domain of retroviral gag proteins and inhibits virion assembly. J Virol 74: 11027-11039.
    • (2000) J Virol , vol.74 , pp. 11027-11039
    • Bacharach, E.1    Gonsky, J.2    Alin, K.3    Orlova, M.4    Goff, S.P.5
  • 40
    • 0034672125 scopus 로고    scopus 로고
    • The cell-surface-expressed nucleolin is associated with the actin cytoskeleton
    • Hovanessian A, Puvion-Dutilleul F, Nisole S, Svab J, Perret E, et al. (2000) The cell-surface-expressed nucleolin is associated with the actin cytoskeleton. Exp Cell Res 261: 312-328.
    • (2000) Exp Cell Res , vol.261 , pp. 312-328
    • Hovanessian, A.1    Puvion-Dutilleul, F.2    Nisole, S.3    Svab, J.4    Perret, E.5
  • 41
    • 0033600836 scopus 로고    scopus 로고
    • The anti-HIV pseudopeptide HB-19 forms a complex with the cell-surface-expressed nucleolin independent of heparan sulfate proteoglycans
    • Nisole S, Krust B, Callebaut C, Guichard G, Muller S, et al. (1999) The anti-HIV pseudopeptide HB-19 forms a complex with the cell-surface-expressed nucleolin independent of heparan sulfate proteoglycans. J Biol Chem 274: 27875-27884.
    • (1999) J Biol Chem , vol.274 , pp. 27875-27884
    • Nisole, S.1    Krust, B.2    Callebaut, C.3    Guichard, G.4    Muller, S.5
  • 42
    • 0037020240 scopus 로고    scopus 로고
    • The anti-HIV cytokine midkine binds the cell surface-expressed nucleolin as a low affinity receptor
    • Said EA, Krust B, Nisole S, Svab J, Briand JP, et al. (2002) The anti-HIV cytokine midkine binds the cell surface-expressed nucleolin as a low affinity receptor. J Biol Chem 277: 37492-37502.
    • (2002) J Biol Chem , vol.277 , pp. 37492-37502
    • Said, E.A.1    Krust, B.2    Nisole, S.3    Svab, J.4    Briand, J.P.5
  • 43
    • 25444530635 scopus 로고    scopus 로고
    • Pleiotrophin inhibits HIV infection by binding the cell surface-expressed nucleolin
    • Said EA, Courty J, Svab J, Delbe J, Krust B, et al. (2005) Pleiotrophin inhibits HIV infection by binding the cell surface-expressed nucleolin. Febs J 272: 4646-4659.
    • (2005) Febs J , vol.272 , pp. 4646-4659
    • Said, E.A.1    Courty, J.2    Svab, J.3    Delbe, J.4    Krust, B.5
  • 46
    • 33749387684 scopus 로고    scopus 로고
    • Cell surface nucleolin on developing muscle is a potential ligand for the axonal receptor protein tyrosine phosphatase-sigma
    • Alete DE, Weeks ME, Hovanession AG, Hawadle M, Stoker AW (2006) Cell surface nucleolin on developing muscle is a potential ligand for the axonal receptor protein tyrosine phosphatase-sigma. FEBS J 273: 4668-4681.
    • (2006) FEBS J , vol.273 , pp. 4668-4681
    • Alete, D.E.1    Weeks, M.E.2    Hovanession, A.G.3    Hawadle, M.4    Stoker, A.W.5
  • 47
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • Hynes NE, Lane HA (2005) ERBB receptors and cancer: the complexity of targeted inhibitors. Nat Rev Cancer 5: 341-354.
    • (2005) Nat Rev Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 48
    • 0032477606 scopus 로고    scopus 로고
    • Haklai R, Weisz MG, Elad G, Paz A, Marciano D, et al. (1998) Dislodgment and accelerated degradation of Ras. Biochemistry 37: 1306-1314.
    • Haklai R, Weisz MG, Elad G, Paz A, Marciano D, et al. (1998) Dislodgment and accelerated degradation of Ras. Biochemistry 37: 1306-1314.


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