메뉴 건너뛰기




Volumn 1808, Issue 1, 2011, Pages 253-259

Specific inhibition of a pathogenic receptor tyrosine kinase by its transmembrane domain

Author keywords

Receptor tyrosine kinase; Signaling; Transmembrane domain

Indexed keywords

FIBROBLAST GROWTH FACTOR RECEPTOR 3; HETERODIMER; MEMBRANE PROTEIN; PROTEIN TYROSINE KINASE;

EID: 78649797430     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.08.007     Document Type: Article
Times cited : (21)

References (47)
  • 1
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • J. Schlessinger Ligand-induced, receptor-mediated dimerization and activation of EGF receptor Cell 110 2002 669 672
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 3
    • 9444287030 scopus 로고    scopus 로고
    • Common and distinct elements in cellular signaling via EGF and FGF receptors
    • J. Schlessinger Common and distinct elements in cellular signaling via EGF and FGF receptors Science 306 2004 1506 1507
    • (2004) Science , vol.306 , pp. 1506-1507
    • Schlessinger, J.1
  • 4
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • X. Zhang, J. Gureasko, K. Shen, P.A. Cole, and J. Kuriyan An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor Cell 125 2006 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
  • 7
    • 0032546031 scopus 로고    scopus 로고
    • Oncogenic activation of the PDGF beta receptor by the transmembrane domain of p185neu*
    • L.M. Petti, P.M. Irusta, and D. DiMaio Oncogenic activation of the PDGF beta receptor by the transmembrane domain of p185neu* Oncogene 16 1998 843 851
    • (1998) Oncogene , vol.16 , pp. 843-851
    • Petti, L.M.1    Irusta, P.M.2    Dimaio, D.3
  • 8
    • 0027186439 scopus 로고
    • Substitution of the erbB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1
    • B. Cheatham, S.E. Shoelson, K. Yamada, E. Goncalves, and C.R. Kahn Substitution of the erbB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1 Proc. Natl. Acad. Sci. U.S.A. 90 1993 7336 7340
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7336-7340
    • Cheatham, B.1    Shoelson, S.E.2    Yamada, K.3    Goncalves, E.4    Kahn, C.R.5
  • 9
    • 0037085373 scopus 로고    scopus 로고
    • The single transmembrane domains of ErbB receptors self-associate in cell membranes
    • J.M. Mendrola, M.B. Berger, M.C. King, and M.A. Lemmon The single transmembrane domains of ErbB receptors self-associate in cell membranes J. Biol. Chem. 277 2002 4704 4712
    • (2002) J. Biol. Chem. , vol.277 , pp. 4704-4712
    • Mendrola, J.M.1    Berger, M.B.2    King, M.C.3    Lemmon, M.A.4
  • 10
    • 52049092046 scopus 로고    scopus 로고
    • Transmembrane domain of EphA1 receptor forms dimers in membrane-like environment
    • E.O. Artemenko, N.S. Egorova, A.S. Arseniev, and A.V. Feofanov Transmembrane domain of EphA1 receptor forms dimers in membrane-like environment Biochim. Biophys. Acta 1778 2008 2361 2367
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2361-2367
    • Artemenko, E.O.1    Egorova, N.S.2    Arseniev, A.S.3    Feofanov, A.V.4
  • 11
    • 68949110276 scopus 로고    scopus 로고
    • Energetics of ErbB1 transmembrane domain dimerization in lipid bilayers
    • L. Chen, M. Merzlyakov, T. Cohen, Y. Shai, and K. Hristova Energetics of ErbB1 transmembrane domain dimerization in lipid bilayers Biophys. J. 96 2009 4622 4630
    • (2009) Biophys. J. , vol.96 , pp. 4622-4630
    • Chen, L.1    Merzlyakov, M.2    Cohen, T.3    Shai, Y.4    Hristova, K.5
  • 12
    • 31344468061 scopus 로고    scopus 로고
    • FGFR3 dimer stabilization due to a single amino acid pathogenic mutation
    • E. Li, M. You, and K. Hristova FGFR3 dimer stabilization due to a single amino acid pathogenic mutation J. Mol. Biol. 356 2006 600 612
    • (2006) J. Mol. Biol. , vol.356 , pp. 600-612
    • Li, E.1    You, M.2    Hristova, K.3
  • 13
    • 73349087177 scopus 로고    scopus 로고
    • The single transmembrane domains of human receptor tyrosine kinases encode self-interactions
    • C. Finger, C. Escher, and D. Schneider The single transmembrane domains of human receptor tyrosine kinases encode self-interactions Sci. Signal 2 2009 ra56
    • (2009) Sci. Signal , vol.2 , pp. 56
    • Finger, C.1    Escher, C.2    Schneider, D.3
  • 14
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • D. Langosch, B. Brosig, H. Kolmar, and H.J. Fritz Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator J. Mol. Biol. 263 1996 525 530
    • (1996) J. Mol. Biol. , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.J.4
  • 15
    • 0942276402 scopus 로고    scopus 로고
    • The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper
    • W. Ruan, V. Becker, U. Klingmuller, and D. Langosch The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper J. Biol. Chem. 279 2004 3273 3279
    • (2004) J. Biol. Chem. , vol.279 , pp. 3273-3279
    • Ruan, W.1    Becker, V.2    Klingmuller, U.3    Langosch, D.4
  • 16
    • 2442647912 scopus 로고    scopus 로고
    • Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization
    • D. Gerber, N. Sal-Man, and Y. Shai Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization J. Biol. Chem. 279 2004 21177 21182
    • (2004) J. Biol. Chem. , vol.279 , pp. 21177-21182
    • Gerber, D.1    Sal-Man, N.2    Shai, Y.3
  • 17
    • 67349094494 scopus 로고    scopus 로고
    • Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains
    • C. Escher, F. Cymer, and D. Schneider Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains J. Mol. Biol. 389 2009 10 16
    • (2009) J. Mol. Biol. , vol.389 , pp. 10-16
    • Escher, C.1    Cymer, F.2    Schneider, D.3
  • 18
    • 15544385324 scopus 로고    scopus 로고
    • Forster resonance energy transfer in liposomes: Measurements of transmembrane helix dimerization in the native bilayer environment
    • M. You, E. Li, W.C. Wimley, and K. Hristova Forster resonance energy transfer in liposomes: measurements of transmembrane helix dimerization in the native bilayer environment Anal. Biochem. 340 2005 154 164
    • (2005) Anal. Biochem. , vol.340 , pp. 154-164
    • You, M.1    Li, E.2    Wimley, W.C.3    Hristova, K.4
  • 19
    • 33645096586 scopus 로고    scopus 로고
    • Transmembrane helix heterodimerization in lipid bilayers: Probing the energetics behind autosomal dominant growth disorders
    • M. Merzlyakov, M. You, E. Li, and K. Hristova Transmembrane helix heterodimerization in lipid bilayers: probing the energetics behind autosomal dominant growth disorders J. Mol. Biol. 358 2006 1 7
    • (2006) J. Mol. Biol. , vol.358 , pp. 1-7
    • Merzlyakov, M.1    You, M.2    Li, E.3    Hristova, K.4
  • 20
    • 58249091559 scopus 로고    scopus 로고
    • Forster resonance energy transfer measurements of transmembrane helix dimerization energetics
    • M. Merzlyakov, and K. Hristova Forster resonance energy transfer measurements of transmembrane helix dimerization energetics Meth. Enzymol. 450 2008 107 127
    • (2008) Meth. Enzymol. , vol.450 , pp. 107-127
    • Merzlyakov, M.1    Hristova, K.2
  • 21
    • 11844249905 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and forster resonance energy transfer suggest weak interactions between fibroblast growth factor receptor 3 (FGFR3) transmembrane domains in the absence of extracellular domains and ligands
    • E. Li, M. You, and K. Hristova Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and forster resonance energy transfer suggest weak interactions between fibroblast growth factor receptor 3 (FGFR3) transmembrane domains in the absence of extracellular domains and ligands Biochemistry 44 2005 352 360
    • (2005) Biochemistry , vol.44 , pp. 352-360
    • Li, E.1    You, M.2    Hristova, K.3
  • 22
    • 0024505028 scopus 로고
    • A point mutation in the neu oncogene mimics ligand induction of receptor aggregation
    • D.B. Weiner, J. Liu, J.A. Cohen, W.V. Williams, and M.I. Greene A point mutation in the neu oncogene mimics ligand induction of receptor aggregation Nature 339 1989 230 231
    • (1989) Nature , vol.339 , pp. 230-231
    • Weiner, D.B.1    Liu, J.2    Cohen, J.A.3    Williams, W.V.4    Greene, M.I.5
  • 23
    • 0030064347 scopus 로고    scopus 로고
    • Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia
    • M.K. Webster, and D.J. Donoghue Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia EMBO J. 15 1996 520 527
    • (1996) EMBO J. , vol.15 , pp. 520-527
    • Webster, M.K.1    Donoghue, D.J.2
  • 24
    • 0028793472 scopus 로고
    • Fibroblast growth factor receptor 3 (FGFR3) transmembrane mutation in Crouzon syndrome with acanthosis nigricans
    • G.A. Meyers, S.J. Orlow, I.R. Munro, K.A. Przylepa, and E.W. Jabs Fibroblast growth factor receptor 3 (FGFR3) transmembrane mutation in Crouzon syndrome with acanthosis nigricans Nat. Genet. 11 1995 462 464
    • (1995) Nat. Genet. , vol.11 , pp. 462-464
    • Meyers, G.A.1    Orlow, S.J.2    Munro, I.R.3    Przylepa, K.A.4    Jabs, E.W.5
  • 25
    • 33646889068 scopus 로고    scopus 로고
    • Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies
    • E. Li, and K. Hristova Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies Biochemistry 45 2006 6241 6251
    • (2006) Biochemistry , vol.45 , pp. 6241-6251
    • Li, E.1    Hristova, K.2
  • 26
    • 77953603192 scopus 로고    scopus 로고
    • Receptor tyrosine kinase transmembrane domains: Function, dimer structure and dimerization energetics
    • E. Li, and K. Hristova Receptor tyrosine kinase transmembrane domains: function, dimer structure and dimerization energetics Cell Adh. Migr. 4 2010 249 254
    • (2010) Cell Adh. Migr. , vol.4 , pp. 249-254
    • Li, E.1    Hristova, K.2
  • 29
    • 0027203585 scopus 로고
    • Specific short transmembrane sequences can inhibit transformation by the mutant neu growth factor receptor in vitro and in vivo
    • F.J. Lofts, H.C. Hurst, M.J. Sternberg, and W.J. Gullick Specific short transmembrane sequences can inhibit transformation by the mutant neu growth factor receptor in vitro and in vivo Oncogene 8 1993 2813 2820
    • (1993) Oncogene , vol.8 , pp. 2813-2820
    • Lofts, F.J.1    Hurst, H.C.2    Sternberg, M.J.3    Gullick, W.J.4
  • 31
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • M.A. Lemmon, and D.M. Engelman Specificity and promiscuity in membrane helix interactions Q. Rev. Biophys. 27 1994 157 218
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 157-218
    • Lemmon, M.A.1    Engelman, D.M.2
  • 32
    • 0025274249 scopus 로고
    • A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization
    • M.J. Sternberg, and W.J. Gullick A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization Protein Eng. 3 1990 245 248
    • (1990) Protein Eng. , vol.3 , pp. 245-248
    • Sternberg, M.J.1    Gullick, W.J.2
  • 33
    • 33751328082 scopus 로고    scopus 로고
    • ErbB receptors: New insights on mechanisms and biology
    • B. Linggi, and G. Carpenter ErbB receptors: new insights on mechanisms and biology Trends Cell Biol. 16 2006 649 656
    • (2006) Trends Cell Biol. , vol.16 , pp. 649-656
    • Linggi, B.1    Carpenter, G.2
  • 35
    • 0034638925 scopus 로고    scopus 로고
    • Molecular mechanisms underlying ErbB2/HER2 action in breast cancer
    • D. Harari, and Y. Yarden Molecular mechanisms underlying ErbB2/HER2 action in breast cancer Oncogene 19 2000 6102 6114
    • (2000) Oncogene , vol.19 , pp. 6102-6114
    • Harari, D.1    Yarden, Y.2
  • 36
    • 0034464005 scopus 로고    scopus 로고
    • The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: The achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with acanthosis nigricans
    • Z. Vajo, C.A. Francomano, and D.J. Wilkin The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: the achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with acanthosis nigricans Endocr. Rev. 21 2000 23 39
    • (2000) Endocr. Rev. , vol.21 , pp. 23-39
    • Vajo, Z.1    Francomano, C.A.2    Wilkin, D.J.3
  • 37
    • 14644394929 scopus 로고    scopus 로고
    • Cell responses to FGFR3 signalling: Growth, differentiation and apoptosis
    • C.G. L'Hote, and M.A. Knowles Cell responses to FGFR3 signalling: growth, differentiation and apoptosis Exp. Cell Res. 304 2005 417 431
    • (2005) Exp. Cell Res. , vol.304 , pp. 417-431
    • L'Hote, C.G.1    Knowles, M.A.2
  • 39
    • 0037861955 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor-3 as a therapeutic target for Achondroplasia-genetic short limbed dwarfism
    • D. Aviezer, M. Golembo, and A. Yayon Fibroblast growth factor receptor-3 as a therapeutic target for Achondroplasia-genetic short limbed dwarfism Curr. Drug Targets 4 2003 353 365
    • (2003) Curr. Drug Targets , vol.4 , pp. 353-365
    • Aviezer, D.1    Golembo, M.2    Yayon, A.3
  • 40
    • 0022485548 scopus 로고
    • Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
    • C.I. Bargmann, M.C. Hung, and R.A. Weinberg Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185 Cell 45 1986 649 657
    • (1986) Cell , vol.45 , pp. 649-657
    • Bargmann, C.I.1    Hung, M.C.2    Weinberg, R.A.3
  • 41
    • 0024042025 scopus 로고
    • Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
    • C.I. Bargmann, and R.A. Weinberg Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion EMBO J. 7 1988 2043 2052
    • (1988) EMBO J. , vol.7 , pp. 2043-2052
    • Bargmann, C.I.1    Weinberg, R.A.2
  • 42
    • 56949102246 scopus 로고    scopus 로고
    • Pathogenic activation of receptor tyrosine kinases in mammalian membranes
    • L. He, and K. Hristova Pathogenic activation of receptor tyrosine kinases in mammalian membranes J. Mol. Biol. 384 2008 1130 1142
    • (2008) J. Mol. Biol. , vol.384 , pp. 1130-1142
    • He, L.1    Hristova, K.2
  • 44
    • 16244374645 scopus 로고    scopus 로고
    • Recombinant antibody expression vectors enabling double and triple immunostaining of tissue culture cells using monoclonal antibodies
    • J.M. Raats, and D. Hof Recombinant antibody expression vectors enabling double and triple immunostaining of tissue culture cells using monoclonal antibodies Eur. J. Cell Biol. 84 2005 517 521
    • (2005) Eur. J. Cell Biol. , vol.84 , pp. 517-521
    • Raats, J.M.1    Hof, D.2
  • 45
    • 0024502540 scopus 로고
    • High-yield trapping of EGF-induced receptor dimers by chemical cross-linking
    • B.O. Fanger, J.E. Stephens, and J.V. Staros High-yield trapping of EGF-induced receptor dimers by chemical cross-linking FASEB J. 3 1989 71 75
    • (1989) FASEB J. , vol.3 , pp. 71-75
    • Fanger, B.O.1    Stephens, J.E.2    Staros, J.V.3
  • 46
    • 0033981302 scopus 로고    scopus 로고
    • The transmembrane mutation G380R in fibroblast growth factor receptor 3 uncouples ligand-mediated receptor activation from down-regulation
    • E. Monsonego-Ornan, R. Adar, T. Feferman, O. Segev, and A. Yayon The transmembrane mutation G380R in fibroblast growth factor receptor 3 uncouples ligand-mediated receptor activation from down-regulation Mol. Cell. Biol. 20 2000 516 522
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 516-522
    • Monsonego-Ornan, E.1    Adar, R.2    Feferman, T.3    Segev, O.4    Yayon, A.5
  • 47
    • 0024395587 scopus 로고
    • Synergistic interaction of p185c-neu and the EGF receptor leads to transformation of rodent fibroblasts
    • Y. Kokai, J.N. Myers, T. Wada, V.I. Brown, C.M. LeVea, J.G. Davis, K. Dobashi, and M.I. Greene Synergistic interaction of p185c-neu and the EGF receptor leads to transformation of rodent fibroblasts Cell 58 1989 287 292
    • (1989) Cell , vol.58 , pp. 287-292
    • Kokai, Y.1    Myers, J.N.2    Wada, T.3    Brown, V.I.4    Levea, C.M.5    Davis, J.G.6    Dobashi, K.7    Greene, M.I.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.