메뉴 건너뛰기




Volumn 19, Issue 2, 2007, Pages 117-123

Receptor tyrosine kinases: mechanisms of activation and signaling

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; ERLOTINIB; GEFITINIB; IMATINIB; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR;

EID: 33847696075     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2007.02.010     Document Type: Review
Times cited : (374)

References (51)
  • 1
    • 0034693799 scopus 로고    scopus 로고
    • The protein tyrosine kinase family of the human genome
    • Robinson D.R., Wu Y.M., and Lin S.F. The protein tyrosine kinase family of the human genome. Oncogene 19 (2000) 5548-5557
    • (2000) Oncogene , vol.19 , pp. 5548-5557
    • Robinson, D.R.1    Wu, Y.M.2    Lin, S.F.3
  • 2
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P., and Hunter T. Oncogenic kinase signalling. Nature 411 (2001) 355-365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 3
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 103 (2000) 211-225
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 4
    • 2942594298 scopus 로고    scopus 로고
    • Juxtamembrane autoinhibition in receptor tyrosine kinases
    • Hubbard S.R. Juxtamembrane autoinhibition in receptor tyrosine kinases. Nat Rev Mol Cell Biol 5 (2004) 464-471
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 464-471
    • Hubbard, S.R.1
  • 5
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • Pawson T., Gish G.D., and Nash P. SH2 domains, interaction modules and cellular wiring. Trends Cell Biol 11 (2001) 504-511
    • (2001) Trends Cell Biol , vol.11 , pp. 504-511
    • Pawson, T.1    Gish, G.D.2    Nash, P.3
  • 7
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki T., Maruyama H., and Maruyama I.N. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J Mol Biol 311 (2001) 1011-1026
    • (2001) J Mol Biol , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 8
    • 33748939242 scopus 로고    scopus 로고
    • Single-molecule analysis of epidermal growth factor binding on the surface of living cells
    • This single-molecule fluorescence study provides quantitative kinetic parameters for the activation of EGFR by EGF.
    • Teramura Y., Ichinose J., Takagi H., Nishida K., Yanagida T., and Sako Y. Single-molecule analysis of epidermal growth factor binding on the surface of living cells. EMBO J 25 (2006) 4215-4222. This single-molecule fluorescence study provides quantitative kinetic parameters for the activation of EGFR by EGF.
    • (2006) EMBO J , vol.25 , pp. 4215-4222
    • Teramura, Y.1    Ichinose, J.2    Takagi, H.3    Nishida, K.4    Yanagida, T.5    Sako, Y.6
  • 10
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • This structural and biochemical study establishes that the EGFR kinase is activated through an allosteric mechanism resembling activation of CDK2 by cyclin A. This study also establishes that the inactive state of the EGFR kinase is Src-like.
    • Zhang X., Gureasko J., Shen K., Cole P.A., and Kuriyan J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125 (2006) 1137-1149. This structural and biochemical study establishes that the EGFR kinase is activated through an allosteric mechanism resembling activation of CDK2 by cyclin A. This study also establishes that the inactive state of the EGFR kinase is Src-like.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 12
    • 33645235265 scopus 로고    scopus 로고
    • Structural basis of hepatocyte growth factor/scatter factor and MET signalling
    • Electron microscopy and small-angle x-ray scattering data are used to develop a structural model for the active 2:2 HGF-Met complex.
    • Gherardi E., Sandin S., Petoukhov M.V., Finch J., Youles M.E., Ofverstedt L.G., Miguel R.N., Blundell T.L., Vande Woude G.F., Skoglund U., et al. Structural basis of hepatocyte growth factor/scatter factor and MET signalling. Proc Natl Acad Sci USA 103 (2006) 4046-4051. Electron microscopy and small-angle x-ray scattering data are used to develop a structural model for the active 2:2 HGF-Met complex.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4046-4051
    • Gherardi, E.1    Sandin, S.2    Petoukhov, M.V.3    Finch, J.4    Youles, M.E.5    Ofverstedt, L.G.6    Miguel, R.N.7    Blundell, T.L.8    Vande Woude, G.F.9    Skoglund, U.10
  • 14
    • 18144423534 scopus 로고    scopus 로고
    • Structural basis for fibroblast growth factor receptor activation
    • Mohammadi M., Olsen S.K., and Ibrahimi O.A. Structural basis for fibroblast growth factor receptor activation. Cytokine Growth Factor Rev 16 (2005) 107-137
    • (2005) Cytokine Growth Factor Rev , vol.16 , pp. 107-137
    • Mohammadi, M.1    Olsen, S.K.2    Ibrahimi, O.A.3
  • 16
    • 33748639228 scopus 로고    scopus 로고
    • Structure of the insulin receptor ectodomain reveals a folded-over conformation
    • Using two different Fab antibody fragments, the entire ectodomain of the insulin receptor is crystallized and its three-dimensional structure solved. Although the structure lacks insulin, it spatially establishes the domain organization within the ectodomain.
    • McKern N.M., Lawrence M.C., Streltsov V.A., Lou M.Z., Adams T.E., Lovrecz G.O., Elleman T.C., Richards K.M., Bentley J.D., Pilling P.A., et al. Structure of the insulin receptor ectodomain reveals a folded-over conformation. Nature 443 (2006) 218-221. Using two different Fab antibody fragments, the entire ectodomain of the insulin receptor is crystallized and its three-dimensional structure solved. Although the structure lacks insulin, it spatially establishes the domain organization within the ectodomain.
    • (2006) Nature , vol.443 , pp. 218-221
    • McKern, N.M.1    Lawrence, M.C.2    Streltsov, V.A.3    Lou, M.Z.4    Adams, T.E.5    Lovrecz, G.O.6    Elleman, T.C.7    Richards, K.M.8    Bentley, J.D.9    Pilling, P.A.10
  • 17
    • 33750264993 scopus 로고    scopus 로고
    • Quantitative analysis of the activation mechanism of the multicomponent growth-factor receptor Ret
    • Using binding and phosphorylation measurements from live cells, along with mathematical modeling, the authors provide a quantitative description of the formation of the ART-Ret-GFRα3 signaling complex.
    • Schlee S., Carmillo P., and Whitty A. Quantitative analysis of the activation mechanism of the multicomponent growth-factor receptor Ret. Nat Chem Biol 2 (2006) 636-644. Using binding and phosphorylation measurements from live cells, along with mathematical modeling, the authors provide a quantitative description of the formation of the ART-Ret-GFRα3 signaling complex.
    • (2006) Nat Chem Biol , vol.2 , pp. 636-644
    • Schlee, S.1    Carmillo, P.2    Whitty, A.3
  • 19
    • 33750805256 scopus 로고    scopus 로고
    • Crystal structure of the agrin-responsive immunoglobulin-like domains 1 and 2 of the receptor tyrosine kinase MuSK
    • Stiegler A.L., Burden S.J., and Hubbard S.R. Crystal structure of the agrin-responsive immunoglobulin-like domains 1 and 2 of the receptor tyrosine kinase MuSK. J Mol Biol 364 (2006) 424-433
    • (2006) J Mol Biol , vol.364 , pp. 424-433
    • Stiegler, A.L.1    Burden, S.J.2    Hubbard, S.R.3
  • 20
    • 0346156078 scopus 로고    scopus 로고
    • Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor
    • Hu J., Liu J., Ghirlando R., Saltiel A.R., and Hubbard S.R. Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor. Mol Cell 12 (2003) 1379-1389
    • (2003) Mol Cell , vol.12 , pp. 1379-1389
    • Hu, J.1    Liu, J.2    Ghirlando, R.3    Saltiel, A.R.4    Hubbard, S.R.5
  • 21
    • 26944466110 scopus 로고    scopus 로고
    • Structural basis for inhibition of the insulin receptor by the adaptor protein Grb14
    • The crystal structure of the complex between the insulin receptor kinase and the BPS region of Grb14 illuminates the mechanism by which Grb14 functions as a negative regulator of insulin signaling; the BPS region acts as a pseudosubstrate inhibitor.
    • Depetris R.S., Hu J., Gimpelevich I., Holt L.J., and Hubbard S.R. Structural basis for inhibition of the insulin receptor by the adaptor protein Grb14. Mol Cell 20 (2005) 325-333. The crystal structure of the complex between the insulin receptor kinase and the BPS region of Grb14 illuminates the mechanism by which Grb14 functions as a negative regulator of insulin signaling; the BPS region acts as a pseudosubstrate inhibitor.
    • (2005) Mol Cell , vol.20 , pp. 325-333
    • Depetris, R.S.1    Hu, J.2    Gimpelevich, I.3    Holt, L.J.4    Hubbard, S.R.5
  • 23
    • 0037429722 scopus 로고    scopus 로고
    • ErbB-4: mechanism of action and biology
    • Carpenter G. ErbB-4: mechanism of action and biology. Exp Cell Res 284 (2003) 66-77
    • (2003) Exp Cell Res , vol.284 , pp. 66-77
    • Carpenter, G.1
  • 24
    • 33749072714 scopus 로고    scopus 로고
    • Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain
    • Sardi S.P., Murtie J., Koirala S., Patten B.A., and Corfas G. Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain. Cell 127 (2006) 185-197
    • (2006) Cell , vol.127 , pp. 185-197
    • Sardi, S.P.1    Murtie, J.2    Koirala, S.3    Patten, B.A.4    Corfas, G.5
  • 25
    • 20344396123 scopus 로고    scopus 로고
    • Eph receptor signalling casts a wide net on cell behaviour
    • Pasquale E.B. Eph receptor signalling casts a wide net on cell behaviour. Nat Rev Mol Cell Biol 6 (2005) 462-475
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 462-475
    • Pasquale, E.B.1
  • 26
    • 0034714357 scopus 로고    scopus 로고
    • Regulated cleavage of a contact-mediated axon repellent
    • Hattori M., Osterfield M., and Flanagan J.G. Regulated cleavage of a contact-mediated axon repellent. Science 289 (2000) 1360-1365
    • (2000) Science , vol.289 , pp. 1360-1365
    • Hattori, M.1    Osterfield, M.2    Flanagan, J.G.3
  • 27
    • 26844448800 scopus 로고    scopus 로고
    • Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans
    • This study provides mechanistic details governing ADAM10 cleavage of ephrinA5-EphA4, which underlies cell-cell repulsion as mediated by ephrin-Eph interactions.
    • Janes P.W., Saha N., Barton W.A., Kolev M.V., Wimmer-Kleikamp S.H., Nievergall E., Blobel C.P., Himanen J.P., Lackmann M., and Nikolov D.B. Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Cell 123 (2005) 291-304. This study provides mechanistic details governing ADAM10 cleavage of ephrinA5-EphA4, which underlies cell-cell repulsion as mediated by ephrin-Eph interactions.
    • (2005) Cell , vol.123 , pp. 291-304
    • Janes, P.W.1    Saha, N.2    Barton, W.A.3    Kolev, M.V.4    Wimmer-Kleikamp, S.H.5    Nievergall, E.6    Blobel, C.P.7    Himanen, J.P.8    Lackmann, M.9    Nikolov, D.B.10
  • 28
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann M. Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Biol 7 (2006) 952-958
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 952-958
    • Mann, M.1
  • 29
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • This paper describes the first in-depth study of the temporal dimension of the EGFR signaling network, using the SILAC proteomic approach. The authors study the tyrosine phosphorylation status of a number of proteins after stimulation with EGF for various periods of time.
    • Blagoev B., Ong S.E., Kratchmarova I., and Mann M. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat Biotechnol 22 (2004) 1139-1145. This paper describes the first in-depth study of the temporal dimension of the EGFR signaling network, using the SILAC proteomic approach. The authors study the tyrosine phosphorylation status of a number of proteins after stimulation with EGF for various periods of time.
    • (2004) Nat Biotechnol , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 30
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • A chemical derivatization strategy is used to study tyrosine phosphorylated proteins in EGF-stimulated cells.
    • Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., and White F.M. Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics 4 (2005) 1240-1250. A chemical derivatization strategy is used to study tyrosine phosphorylated proteins in EGF-stimulated cells.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4    Rush, J.5    Lauffenburger, D.A.6    White, F.M.7
  • 31
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • An expanded proteomics study of the EGF signaling network in which the phosphorylation of 2,244 proteins at 6,600 tyrosine, serine, and threonine sites is reported. The data from this study have been compiled into a publicly accessible database called Phosida (http://www.phosida.com).
    • Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., and Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127 (2006) 635-648. An expanded proteomics study of the EGF signaling network in which the phosphorylation of 2,244 proteins at 6,600 tyrosine, serine, and threonine sites is reported. The data from this study have been compiled into a publicly accessible database called Phosida (http://www.phosida.com).
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 32
    • 33644836196 scopus 로고    scopus 로고
    • Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC)
    • Zhang G., Spellman D.S., Skolnik E.Y., and Neubert T.A. Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC). J Proteome Res 5 (2006) 581-588
    • (2006) J Proteome Res , vol.5 , pp. 581-588
    • Zhang, G.1    Spellman, D.S.2    Skolnik, E.Y.3    Neubert, T.A.4
  • 33
    • 33749332751 scopus 로고    scopus 로고
    • Temporal dynamics of tyrosine phosphorylation in insulin signaling
    • Schmelzle K., Kane S., Gridley S., Lienhard G.E., and White F.M. Temporal dynamics of tyrosine phosphorylation in insulin signaling. Diabetes 55 (2006) 2171-2179
    • (2006) Diabetes , vol.55 , pp. 2171-2179
    • Schmelzle, K.1    Kane, S.2    Gridley, S.3    Lienhard, G.E.4    White, F.M.5
  • 35
    • 33846009481 scopus 로고    scopus 로고
    • A phosphoproteomic analysis of the ErbB2 receptor tyrosine kinase signaling pathways
    • Mukherji M., Brill L.M., Ficarro S.B., Hampton G.M., and Schultz P.G. A phosphoproteomic analysis of the ErbB2 receptor tyrosine kinase signaling pathways. Biochemistry 45 (2006) 15529-15540
    • (2006) Biochemistry , vol.45 , pp. 15529-15540
    • Mukherji, M.1    Brill, L.M.2    Ficarro, S.B.3    Hampton, G.M.4    Schultz, P.G.5
  • 36
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • Protein microarrays are used to measure the strength of interaction between purified SH2 or PTB domains and phosphotyrosine-containing peptides representing the autophosphorylation sites on ErbB1-4. The data reveal the degree of selectivity for different autophosphorylation sites at different thresholds of affinity.
    • Jones R.B., Gordus A., Krall J.A., and MacBeath G. A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature 439 (2006) 168-174. Protein microarrays are used to measure the strength of interaction between purified SH2 or PTB domains and phosphotyrosine-containing peptides representing the autophosphorylation sites on ErbB1-4. The data reveal the degree of selectivity for different autophosphorylation sites at different thresholds of affinity.
    • (2006) Nature , vol.439 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 37
    • 33747769612 scopus 로고    scopus 로고
    • Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains
    • Dierck K., Machida K., Voigt A., Thimm J., Horstmann M., Fiedler W., Mayer B.J., and Nollau P. Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains. Nat Methods 3 (2006) 737-744
    • (2006) Nat Methods , vol.3 , pp. 737-744
    • Dierck, K.1    Machida, K.2    Voigt, A.3    Thimm, J.4    Horstmann, M.5    Fiedler, W.6    Mayer, B.J.7    Nollau, P.8
  • 38
    • 33750887331 scopus 로고    scopus 로고
    • A functional RNAi screen for regulators of receptor tyrosine kinase and ERK signalling
    • A functional genomics study in D. melanogaster cells that identifies genes involved in positive or negative regulation of ERK following RTK stimulation.
    • Friedman A., and Perrimon N. A functional RNAi screen for regulators of receptor tyrosine kinase and ERK signalling. Nature 444 (2006) 230-234. A functional genomics study in D. melanogaster cells that identifies genes involved in positive or negative regulation of ERK following RTK stimulation.
    • (2006) Nature , vol.444 , pp. 230-234
    • Friedman, A.1    Perrimon, N.2
  • 43
    • 4444344330 scopus 로고    scopus 로고
    • EGF receptor gene mutations are common in lung cancers from 'never smokers' and are associated with sensitivity of tumors to gefitinib and erlotinib
    • Pao W., Miller V., Zakowski M., Doherty J., Politi K., Sarkaria I., Singh B., Heelan R., Rusch V., Fulton L., et al. EGF receptor gene mutations are common in lung cancers from 'never smokers' and are associated with sensitivity of tumors to gefitinib and erlotinib. Proc Natl Acad Sci U S A 101 (2004) 13306-13311
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13306-13311
    • Pao, W.1    Miller, V.2    Zakowski, M.3    Doherty, J.4    Politi, K.5    Sarkaria, I.6    Singh, B.7    Heelan, R.8    Rusch, V.9    Fulton, L.10
  • 44
    • 0035800507 scopus 로고    scopus 로고
    • Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification
    • Gorre M.E., Mohammed M., Ellwood K., Hsu N., Paquette R., Rao P.N., and Sawyers C.L. Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification. Science 293 (2001) 876-880
    • (2001) Science , vol.293 , pp. 876-880
    • Gorre, M.E.1    Mohammed, M.2    Ellwood, K.3    Hsu, N.4    Paquette, R.5    Rao, P.N.6    Sawyers, C.L.7
  • 47
    • 33746258750 scopus 로고    scopus 로고
    • A general strategy for creating 'inactive-conformation' abl inhibitors
    • A structure-based drug design study is reported that describes how novel ATP-competitive inhibitors can be designed to target the inactive conformation of protein kinases, in this case Abl; in general, inactive-state inhibitors exhibit higher specificity and affinity than active-state inhibitors.
    • Okram B., Nagle A., Adrian F.J., Lee C., Ren P., Wang X., Sim T., Xie Y., Xia G., Spraggon G., et al. A general strategy for creating 'inactive-conformation' abl inhibitors. Chem Biol 13 (2006) 779-786. A structure-based drug design study is reported that describes how novel ATP-competitive inhibitors can be designed to target the inactive conformation of protein kinases, in this case Abl; in general, inactive-state inhibitors exhibit higher specificity and affinity than active-state inhibitors.
    • (2006) Chem Biol , vol.13 , pp. 779-786
    • Okram, B.1    Nagle, A.2    Adrian, F.J.3    Lee, C.4    Ren, P.5    Wang, X.6    Sim, T.7    Xie, Y.8    Xia, G.9    Spraggon, G.10
  • 49
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J., and Lemmon M.A. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell 11 (2003) 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    Lemmon, M.A.6
  • 50
    • 33847717293 scopus 로고    scopus 로고
    • Structure of the EGF receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • Stamos J., Sliwkowski M.X., and Eigenbrot C. Structure of the EGF receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J Biol Chem 23 (2002) 23
    • (2002) J Biol Chem , vol.23 , pp. 23
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.