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Volumn 3, Issue 2, 2011, Pages 2032-2049

Glioma specific extracellular missense mutations in the first cysteine rich region of epidermal growth factor receptor (EGFR) initiate ligand independent activation

Author keywords

Autoactivation; DE2 7EGFR; Dimerization; Disulfide bond; EGFR; Extracellular domain mutation; Free cysteine

Indexed keywords

CYSTEINE; EPIDERMAL GROWTH FACTOR RECEPTOR;

EID: 79959733559     PISSN: None     EISSN: 20726694     Source Type: Journal    
DOI: 10.3390/cancers3022032     Document Type: Article
Times cited : (34)

References (32)
  • 1
    • 33751328082 scopus 로고    scopus 로고
    • ErbB receptors: New insights on mechanisms and biology
    • Linggi, B.; Carpenter, G. ErbB receptors: New insights on mechanisms and biology. Tr. Cell Biol. 2006, 16, 649-656.
    • (2006) Tr. Cell Biol , vol.16 , pp. 649-656
    • Linggi, B.1    Carpenter, G.2
  • 3
    • 18644370411 scopus 로고    scopus 로고
    • Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha
    • Garrett, T.P.; McKern, N.M.; Lou, M.; Elleman, T.C.; Adams, T.E.; Lovrecz, G.O.; Zhu, H.J.; Walker, F.; Frenkel, M.J.; Hoyne, P.A.; et al. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha. Cell 2002, 110, 763-773.
    • (2002) Cell , vol.110 , pp. 763-773
    • Garrett, T.P.1    McKern, N.M.2    Lou, M.3    Elleman, T.C.4    Adams, T.E.5    Lovrecz, G.O.6    Zhu, H.J.7    Walker, F.8    Frenkel, M.J.9    Hoyne, P.A.10
  • 5
    • 78349232462 scopus 로고    scopus 로고
    • Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases
    • Bae, J.H.; Schlessinger, J. Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases. Mol. Cells 2010, 29 443-448.
    • (2010) Mol. Cells , vol.29 , pp. 443-448
    • Bae, J.H.1    Schlessinger, J.2
  • 6
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control of EGF receptor activation by reversible dimerization on living cells
    • Chung, I.; Akita, R.; Vandlen, R.; Toomre, D.; Schlessinger, J.; Mellman, I. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 2010, 464, 783-787.
    • (2010) Nature , vol.464 , pp. 783-787
    • Chung, I.1    Akita, R.2    Vandlen, R.3    Toomre, D.4    Schlessinger, J.5    Mellman, I.6
  • 7
    • 67349137902 scopus 로고    scopus 로고
    • The EGFRvIII variant in glioblastoma multiforme
    • Gan, H.K.; Kaye, A.H.; Luwor, R.B. The EGFRvIII variant in glioblastoma multiforme. J. Clin. Neurosci. 2009, 16 748-754.
    • (2009) J. Clin. Neurosci , vol.16 , pp. 748-754
    • Gan, H.K.1    Kaye, A.H.2    Luwor, R.B.3
  • 8
    • 0034954124 scopus 로고    scopus 로고
    • The type III epidermal growth factor receptor mutation. Biological significance and potential target for anti-cancer therapy
    • Pedersen, M.W.; Meltorn, M.; Damstrup, L.; Poulsen, H. S. The type III epidermal growth factor receptor mutation. Biological significance and potential target for anti-cancer therapy. Ann. Oncol. 2001, 12, 745-760.
    • (2001) Ann. Oncol , vol.12 , pp. 745-760
    • Pedersen, M.W.1    Meltorn, M.2    Damstrup, L.3    Poulsen, H.S.4
  • 9
    • 0037139359 scopus 로고    scopus 로고
    • Novel monoclonal antibody specific for the de2-7 epidermal growth factor receptor (EGFR) that also recognizes the EGFR expressed in cells containing amplification of the EGFR gene
    • Johns, T.G.; Stockert, E.; Ritter, G.; Jungbluth, A.A.; Huang, H.J.; Cavenee, W.K.; Smyth, F.E.; Hall, C.M.; Watson, N.; Nice, E.C.; et al. Novel monoclonal antibody specific for the de2-7 epidermal growth factor receptor (EGFR) that also recognizes the EGFR expressed in cells containing amplification of the EGFR gene. Int. J. Cancer 2002, 98, 398-408.
    • (2002) Int. J. Cancer , vol.98 , pp. 398-408
    • Johns, T.G.1    Stockert, E.2    Ritter, G.3    Jungbluth, A.A.4    Huang, H.J.5    Cavenee, W.K.6    Smyth, F.E.7    Hall, C.M.8    Watson, N.9    Nice, E.C.10
  • 11
    • 3142657314 scopus 로고    scopus 로고
    • Identification of the epitope for the epidermal growth factor receptor-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor
    • Johns, T.G.; Adams, T.E.; Cochran, J.R.; Hall, N.E.; Hoyne, P.A.; Olsen, M.J.; Kim, Y.S.; Rothacker, J.; Nice, E.C.; Walker, F.; et al. Identification of the epitope for the epidermal growth factor receptor-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor. J. Biol. Chem. 2004, 279, 30375-30384.
    • (2004) J. Biol. Chem , vol.279 , pp. 30375-30384
    • Johns, T.G.1    Adams, T.E.2    Cochran, J.R.3    Hall, N.E.4    Hoyne, P.A.5    Olsen, M.J.6    Kim, Y.S.7    Rothacker, J.8    Nice, E.C.9    Walker, F.10
  • 13
    • 54549108740 scopus 로고    scopus 로고
    • Comprehensive genomic characterization defines human glioblastoma genes and core pathways
    • The Cancer Genome Atlas Research Network
    • The Cancer Genome Atlas Research Network. Comprehensive genomic characterization defines human glioblastoma genes and core pathways. Nature 2008, 455, 1061-1068.
    • (2008) Nature , vol.455 , pp. 1061-1068
  • 14
    • 14444288522 scopus 로고    scopus 로고
    • The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling
    • Huang, H.S.; Nagane, M.; Klingbeil, C.K.; Lin, H.; Nishikawa, R.; Ji, X.D.; Huang, C.M.; Gill, G.N.; Wiley, H.S.; Cavenee, W.K. The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling. J. Biol. Chem. 1997, 272, 2927-2935.
    • (1997) J. Biol. Chem , vol.272 , pp. 2927-2935
    • Huang, H.S.1    Nagane, M.2    Klingbeil, C.K.3    Lin, H.4    Nishikawa, R.5    Ji, X.D.6    Huang, C.M.7    Gill, G.N.8    Wiley, H.S.9    Cavenee, W.K.10
  • 15
    • 0033587604 scopus 로고    scopus 로고
    • Epidermal growth factor receptor internalization rate is regulated by negative charges near the SH2 binding site Tyr992
    • Holbrook, M.R.; O'Donnell, J.B., Jr.; Slakey, L.L.; Gross, D.J. Epidermal growth factor receptor internalization rate is regulated by negative charges near the SH2 binding site Tyr992. Biochemistry 1999, 38, 9348-9356.
    • (1999) Biochemistry , vol.38 , pp. 9348-9356
    • Holbrook, M.R.1    O'Donnell Jr., J.B.2    Slakey, L.L.3    Gross, D.J.4
  • 18
    • 4444263448 scopus 로고    scopus 로고
    • The tumor-specific de2-7 epidermal growth factor receptor (EGFR) promotes cells survival and heterodimerizes with the wild-type EGFR
    • Luwor, R.B.; Zhu, H.J.; Walker, F.; Vitali, A.A.; Perera, R.M.; Burgess, A.W.; Scott, A.M.; Johns, T.G. The tumor-specific de2-7 epidermal growth factor receptor (EGFR) promotes cells survival and heterodimerizes with the wild-type EGFR. Oncogene 2004, 23, 6095-6104.
    • (2004) Oncogene , vol.23 , pp. 6095-6104
    • Luwor, R.B.1    Zhu, H.J.2    Walker, F.3    Vitali, A.A.4    Perera, R.M.5    Burgess, A.W.6    Scott, A.M.7    Johns, T.G.8
  • 19
    • 0030787340 scopus 로고    scopus 로고
    • Receptor dimerization is not a factor in the signalling activity of a transforming variant epidermal growth factor receptor (EGFRvIII)
    • Chu, C.T.; Everiss, K.D.; Wikstrand, C.J.; Batra, S.K.; Kung, H.J.; Bigner, D.D. Receptor dimerization is not a factor in the signalling activity of a transforming variant epidermal growth factor receptor (EGFRvIII). Biochem. J. 1997, 324, 855-861.
    • (1997) Biochem. J , vol.324 , pp. 855-861
    • Chu, C.T.1    Everiss, K.D.2    Wikstrand, C.J.3    Batra, S.K.4    Kung, H.J.5    Bigner, D.D.6
  • 20
    • 0029666423 scopus 로고    scopus 로고
    • Transformational and altered signal transduction by a naturally occurring mutant EGF receptor
    • Moscatello, D.K.; Montgomery, R.B.; Sundareshan, P.; McDanel, H.; Wong, M.Y.; Wong, A.J. Transformational and altered signal transduction by a naturally occurring mutant EGF receptor. Oncogene 1996, 13, 85-96.
    • (1996) Oncogene , vol.13 , pp. 85-96
    • Moscatello, D.K.1    Montgomery, R.B.2    Sundareshan, P.3    McDanel, H.4    Wong, M.Y.5    Wong, A.J.6
  • 21
    • 0035895916 scopus 로고    scopus 로고
    • Glycosylation-induced conformational modification positively regulates receptor-receptor association: A study with an aberrant epidermal growth factor receptor (EGFRvIII/DeltaEGFR) expressed in cancer cells
    • Fernandes, H.; Cohen, S.; Bishayee, S. Glycosylation-induced conformational modification positively regulates receptor-receptor association: A study with an aberrant epidermal growth factor receptor (EGFRvIII/DeltaEGFR) expressed in cancer cells. J. Biol. Chem. 2001, 276, 5375-5383.
    • (2001) J. Biol. Chem , vol.276 , pp. 5375-5383
    • Fernandes, H.1    Cohen, S.2    Bishayee, S.3
  • 22
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang, X.; Gureasko, J.; Shen, K.; Cole, P. A.; Kuriyan, J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 2006, 125, 1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 23
    • 34047273010 scopus 로고    scopus 로고
    • The epidermal growth factor receptor (EGFR) tyrosine kinase inhibitor AG1478 increases the formation of inactive untethered EGFR dimers. Implications for combination therapy with monoclonal antibody 806
    • Gan, H.K.; Walker, F.; Burgess, A.W.; Rigopoulos, A.; Scott, A.M.; Johns, T.G. The epidermal growth factor receptor (EGFR) tyrosine kinase inhibitor AG1478 increases the formation of inactive untethered EGFR dimers. Implications for combination therapy with monoclonal antibody 806. J. Biol. Chem. 2007, 282, 2840-2850.
    • (2007) J. Biol. Chem , vol.282 , pp. 2840-2850
    • Gan, H.K.1    Walker, F.2    Burgess, A.W.3    Rigopoulos, A.4    Scott, A.M.5    Johns, T.G.6
  • 24
    • 33750028210 scopus 로고    scopus 로고
    • A structural model of the extracellular domain of the oncogenic EGFR variant Xmrk
    • Meierjohann, S.; Mueller, T.; Schartl, M.; Buehner, M. A structural model of the extracellular domain of the oncogenic EGFR variant Xmrk. Zebrafish 2006, 3, 59-69.
    • (2006) Zebrafish , vol.3 , pp. 59-69
    • Meierjohann, S.1    Mueller, T.2    Schartl, M.3    Buehner, M.4
  • 25
    • 0032515975 scopus 로고    scopus 로고
    • Activating mutations in the extracellular domain of the fibroblast growth factor receptor 2 function by disruption of the disulfide bond in the third immunoglobulin-like domain
    • Robertson, S.C.; Meyer, A.N.; Hart, K.C.; Galvin, B.D.; Webster, M.K.; Donoghue, D.J. Activating mutations in the extracellular domain of the fibroblast growth factor receptor 2 function by disruption of the disulfide bond in the third immunoglobulin-like domain. Proc. Natl. Acad. Sci. USA 1998, 95, 4567-4572.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4567-4572
    • Robertson, S.C.1    Meyer, A.N.2    Hart, K.C.3    Galvin, B.D.4    Webster, M.K.5    Donoghue, D.J.6
  • 27
    • 0026326555 scopus 로고
    • An activating mutation in the murine erythropoietin receptor induces erythroleukemia in mice: A cytokine receptor superfamily oncogene
    • Longmore, G.D.; Lodish, H.F. An activating mutation in the murine erythropoietin receptor induces erythroleukemia in mice: a cytokine receptor superfamily oncogene. Cell 1991, 67, 1089-1102.
    • (1991) Cell , vol.67 , pp. 1089-1102
    • Longmore, G.D.1    Lodish, H.F.2
  • 28
    • 0030871359 scopus 로고    scopus 로고
    • Mutation associated with Crouzon syndrome causes ligand-independent dimerization and activation of FGF receptor-2
    • Mangasarian, K.; Li, Y.; Mansukhani, A.; Basilico, C. Mutation associated with Crouzon syndrome causes ligand-independent dimerization and activation of FGF receptor-2. J. Cell. Physiol. 1997, 172, 117-125.
    • (1997) J. Cell. Physiol , vol.172 , pp. 117-125
    • Mangasarian, K.1    Li, Y.2    Mansukhani, A.3    Basilico, C.4
  • 30
    • 65949106827 scopus 로고    scopus 로고
    • The plasticity of oncogene addiction: Implications for targeted therapies directed to receptor tyrosine kinases
    • Pillay, V.; Allaf, L.; Wilding, A.L.; Donoghue, J.F.; Court, N.W.; Greenall, S.A.; Scott, A.M.; Johns, T.G. The plasticity of oncogene addiction: implications for targeted therapies directed to receptor tyrosine kinases. Neoplasia 2009, 11, 448-458.
    • (2009) Neoplasia , vol.11 , pp. 448-458
    • Pillay, V.1    Allaf, L.2    Wilding, A.L.3    Donoghue, J.F.4    Court, N.W.5    Greenall, S.A.6    Scott, A.M.7    Johns, T.G.8
  • 31
    • 0029838204 scopus 로고    scopus 로고
    • Mutations affecting conserved cysteine residues within the extracellular domain of Neu promote receptor dimerization and activation
    • Siegel, P.M.; Muller, W.J. Mutations affecting conserved cysteine residues within the extracellular domain of Neu promote receptor dimerization and activation. Proc. Natl. Acad. Sci. USA 1996, 93, 8878-8883.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8878-8883
    • Siegel, P.M.1    Muller, W.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.