메뉴 건너뛰기




Volumn 5, Issue APRIL2016, 2016, Pages

Time-resolved multimodal analysis of src homology 2 (SH2) domain binding in signaling by receptor tyrosine kinases

Author keywords

[No Author keywords available]

Indexed keywords

CRK LIKE PROTEIN; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; PHOSPHOLIPASE C GAMMA1; PROTEIN SH2; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE SHP 2; PROTEIN BINDING;

EID: 84964545756     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.11835     Document Type: Article
Times cited : (21)

References (59)
  • 2
    • 0020039865 scopus 로고
    • Epidermal growth factor inhibits growth of A431 human epidermoid carcinoma in serum-free cell culture
    • Barnes DW. 1982. Epidermal growth factor inhibits growth of A431 human epidermoid carcinoma in serum-free cell culture. The Journal of Cell Biology 93:1-4. doi: 10.1083/jcb.93.1.1
    • (1982) The Journal of Cell Biology , vol.93 , pp. 1-4
    • Barnes, D.W.1
  • 3
    • 0017664223 scopus 로고
    • Physics of chemoreception
    • Berg HC, Purcell EM. 1977. Physics of chemoreception. Biophysical Journal 20:193-219. doi: 10.1016/S0006-3495(77)85544-6
    • (1977) Biophysical Journal , vol.20 , pp. 193-219
    • Berg, H.C.1    Purcell, E.M.2
  • 5
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev B, Kratchmarova I, Ong SE, Nielsen M, Foster LJ, Mann M. 2003. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nature Biotechnology 21:315-318. doi: 10. 1038/nbt790
    • (2003) Nature Biotechnology , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 6
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev B, Ong SE, Kratchmarova I, Mann M. 2004. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nature Biotechnology 22:1139-1145. doi: 10.1038/nbt1005
    • (2004) Nature Biotechnology , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 7
    • 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. 2010. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 464:783-787. doi: 10.1038/nature08827
    • (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
  • 8
    • 84922986379 scopus 로고    scopus 로고
    • MARQUIS: A multiplex method for absolute quantification of peptides and posttranslational modifications
    • Curran TG, Zhang Y, Ma DJ, Sarkaria JN, White FM. 2015. MARQUIS: A multiplex method for absolute quantification of peptides and posttranslational modifications. Nature Communications 6:5924. doi: 10.1038/ ncomms6924
    • (2015) Nature Communications , vol.6 , pp. 5924
    • Curran, T.G.1    Zhang, Y.2    Ma, D.J.3    Sarkaria, J.N.4    White, F.M.5
  • 9
    • 84921827802 scopus 로고    scopus 로고
    • Single-molecule tracking of small GTPase Rac1 uncovers spatial regulation of membrane translocation and mechanism for polarized signaling
    • Das S, Yin T, Yang Q, Zhang J, Wu YI, Yu J. 2015. Single-molecule tracking of small GTPase Rac1 uncovers spatial regulation of membrane translocation and mechanism for polarized signaling. Proceedings of the National Academy of Sciences of the United States of America 112:E267-276. doi: 10.1073/pnas.1409667112
    • (2015) Proceedings of the National Academy of Sciences of the United States of America , vol.112 , pp. 267-276
    • Das, S.1    Yin, T.2    Yang, Q.3    Zhang, J.4    Wu, Y.I.5    Yu, J.6
  • 11
    • 84918821228 scopus 로고    scopus 로고
    • Ultrasensitivity part III: Cascades, bistable switches, and oscillators
    • Ferrell JE, Ha SH. 2014. Ultrasensitivity part III: cascades, bistable switches, and oscillators. Trends in Biochemical Sciences 39:612-618. doi: 10.1016/j.tibs.2014.10.002
    • (2014) Trends in Biochemical Sciences , vol.39 , pp. 612-618
    • Ferrell, J.E.1    Ha, S.H.2
  • 12
    • 0019861187 scopus 로고
    • Increased phosphotyrosine content and inhibition of proliferation in EGF-treated A431 cells
    • Gill GN, Lazar CS. 1981. Increased phosphotyrosine content and inhibition of proliferation in EGF-treated A431 cells. Nature 293:305-307. doi: 10.1038/293305a0
    • (1981) Nature , vol.293 , pp. 305-307
    • Gill, G.N.1    Lazar, C.S.2
  • 14
    • 0030962699 scopus 로고    scopus 로고
    • Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes
    • Harmer SL, DeFranco AL. 1997. Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes. Molecular and Cellular Biology 17:4087-4095. doi: 10.1128/mcb.17.7.4087
    • (1997) Molecular and Cellular Biology , vol.17 , pp. 4087-4095
    • Harmer, S.L.1    DeFranco, A.L.2
  • 15
    • 84866052943 scopus 로고    scopus 로고
    • Comprehensive binary interaction mapping of SH2 domains via fluorescence polarization reveals novel functional diversification of ErbB receptors
    • Hause RJ, Leung KK, Barkinge JL, Ciaccio MF, Chuu CP, Jones RB. 2012. Comprehensive binary interaction mapping of SH2 domains via fluorescence polarization reveals novel functional diversification of ErbB receptors. PloS One 7:e44471. doi: 10.1371/journal.pone.0044471
    • (2012) PloS One , vol.7 , pp. 44471
    • Hause, R.J.1    Leung, K.K.2    Barkinge, J.L.3    Ciaccio, M.F.4    Chuu, C.P.5    Jones, R.B.6
  • 16
    • 0030028790 scopus 로고    scopus 로고
    • A Grb2-associated docking protein in EGF- and insulin-receptor signalling
    • Holgado-Madruga M, Emlet DR, Moscatello DK, Godwin AK, Wong AJ. 1996. A Grb2-associated docking protein in EGF- and insulin-receptor signalling. Nature 379:560-564. doi: 10.1038/379560a0
    • (1996) Nature , vol.379 , pp. 560-564
    • Holgado-Madruga, M.1    Emlet, D.R.2    Moscatello, D.K.3    Godwin, A.K.4    Wong, A.J.5
  • 17
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck PV, Kornhauser JM, Tkachev S, Zhang B, Skrzypek E, Murray B, Latham V, Sullivan M. 2012. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Research 40:D261-D270. doi: 10. 1093/nar/gkr1122
    • (2012) Nucleic Acids Research , vol.40 , pp. D261-D270
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 22
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • Jones RB, Gordus A, Krall JA, MacBeath G. 2006. A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature 439:168-174. doi: 10.1038/nature04177
    • (2006) Nature , vol.439 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 24
    • 0037079054 scopus 로고    scopus 로고
    • Computational systems biology
    • Kitano H. 2002. Computational systems biology. Nature 420:206-210. doi: 10.1038/nature01254
    • (2002) Nature , vol.420 , pp. 206-210
    • Kitano, H.1
  • 25
    • 0027504198 scopus 로고
    • Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells
    • Kusumi A, Sako Y, Yamamoto M. 1993. Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells. Biophysical Journal 65:2021-2040. doi: 10.1016/S0006-3495(93)81253-0
    • (1993) Biophysical Journal , vol.65 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 26
    • 0031910469 scopus 로고    scopus 로고
    • Theory for ligand rebinding at cell membrane surfaces
    • Lagerholm BC, Thompson NL. 1998. Theory for ligand rebinding at cell membrane surfaces. Biophysical Journal 74:1215-1228. doi: 10.1016/S0006-3495(98)77836-1
    • (1998) Biophysical Journal , vol.74 , pp. 1215-1228
    • Lagerholm, B.C.1    Thompson, N.L.2
  • 28
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J. 2010. Cell signaling by receptor tyrosine kinases. Cell 141:1117-1134. doi: 10. 1016/j.cell.2010.06.011
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 29
    • 0020504930 scopus 로고
    • Analysis of morphology and receptor metabolism in clonal variant A431 cells with differing growth responses to epidermal growth factor
    • Lifshitz A, Lazar CS, Buss JE, Gill GN. 1983. Analysis of morphology and receptor metabolism in clonal variant A431 cells with differing growth responses to epidermal growth factor. Journal of Cellular Physiology 115:235-242. doi: 10.1002/jcp.1041150304
    • (1983) Journal of Cellular Physiology , vol.115 , pp. 235-242
    • Lifshitz, A.1    Lazar, C.S.2    Buss, J.E.3    Gill, G.N.4
  • 30
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling
    • Liu BA, Jablonowski K, Raina M, Arcé M, Pawson T, Nash PD. 2006. The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Molecular Cell 22:851-868. doi: 10. 1016/j.molcel.2006.06.001
    • (2006) Molecular Cell , vol.22 , pp. 851-868
    • Liu, B.A.1    Jablonowski, K.2    Raina, M.3    Arcé, M.4    Pawson, T.5    Nash, P.D.6
  • 33
    • 78149463029 scopus 로고    scopus 로고
    • Characterizing tyrosine phosphorylation signaling in lung cancer using SH2 profiling
    • Machida K, Eschrich S, Li J, Bai Y, Koomen J, Mayer BJ, Haura EB. 2010. Characterizing tyrosine phosphorylation signaling in lung cancer using SH2 profiling. PLoS One 5:e13470. doi: 10.1371/journal.pone.0013470
    • (2010) PLoS One , vol.5 , pp. 13470
    • Machida, K.1    Eschrich, S.2    Li, J.3    Bai, Y.4    Koomen, J.5    Mayer, B.J.6    Haura, E.B.7
  • 36
  • 38
    • 0028034549 scopus 로고
    • Grb2/Ash binds directly to tyrosines 1068 and 1086 and indirectly to tyrosine 1148 of activated human epidermal growth factor receptors in intact cells
    • Okutani T, Okabayashi Y, Kido Y, Sugimoto Y, Sakaguchi K, Matuoka K, Takenawa T, Kasuga M. 1994. Grb2/Ash binds directly to tyrosines 1068 and 1086 and indirectly to tyrosine 1148 of activated human epidermal growth factor receptors in intact cells. The Journal of Biological Chemistry 269:31310-31314.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 31310-31314
    • Okutani, T.1    Okabayashi, Y.2    Kido, Y.3    Sugimoto, Y.4    Sakaguchi, K.5    Matuoka, K.6    Takenawa, T.7    Kasuga, M.8
  • 39
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M. 2006. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127:635-648. doi: 10.1016/j.cell.2006.09.026
    • (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
  • 40
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: From phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson T. 2004. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 116:191-203.
    • (2004) Cell , vol.116 , pp. 191-203
    • Pawson, T.1
  • 41
    • 33847285870 scopus 로고    scopus 로고
    • Oncogenic re-wiring of cellular signaling pathways
    • Pawson T, Warner N. 2007. Oncogenic re-wiring of cellular signaling pathways. Oncogene 26:1268-1275. doi:10.1038/sj.onc.1210255
    • (2007) Oncogene , vol.26 , pp. 1268-1275
    • Pawson, T.1    Warner, N.2
  • 43
    • 84890041471 scopus 로고    scopus 로고
    • The ErbB/HER family of protein-tyrosine kinases and cancer
    • Roskoski R. 2014. The ErbB/HER family of protein-tyrosine kinases and cancer. Pharmacological Research 79:34-74. doi: 10.1016/j.phrs.2013.11.002
    • (2014) Pharmacological Research , vol.79 , pp. 34-74
    • Roskoski, R.1
  • 44
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai R, Iwamatsu A, Hirano N, Ogawa S, Tanaka T, Mano H, Yazaki Y, Hirai H. 1994. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. The EMBO Journal 13:3748-3756.
    • (1994) The EMBO Journal , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 45
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako Y, Minoghchi S, Yanagida T. 2000. Single-molecule imaging of EGFR signalling on the surface of living cells. Nature Cell Biology 2:168-172. doi: 10.1038/35004044
    • (2000) Nature Cell Biology , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 46
    • 84855943889 scopus 로고    scopus 로고
    • Ligand-induced clustering of EGF receptors: A quantitative study by fluorescence image moment analysis
    • Sergeev M, Swift JL, Godin AG, Wiseman PW. 2012. Ligand-induced clustering of EGF receptors: a quantitative study by fluorescence image moment analysis. Biophysical Chemistry 161:50-53. doi: 10.1016/j.bpc.2011.11. 003
    • (2012) Biophysical Chemistry , vol.161 , pp. 50-53
    • Sergeev, M.1    Swift, J.L.2    Godin, A.G.3    Wiseman, P.W.4
  • 48
    • 79960610118 scopus 로고    scopus 로고
    • REVIGO summarizes and visualizes long lists of gene ontology terms
    • Supek F, Bošnjak M, Š kunca N, Š muc T. 2011. REVIGO summarizes and visualizes long lists of gene ontology terms. PloS One 6:e21800. doi: 10.1371/journal.pone.0021800
    • (2011) PloS One , vol.6 , pp. 21800
    • Supek, F.1    Bošnjak, M.2    Škunca, N.3    Šmuc, T.4
  • 49
    • 33748939242 scopus 로고    scopus 로고
    • Single-molecule analysis of epidermal growth factor binding on the surface of living cells
    • Teramura Y, Ichinose J, Takagi H, Nishida K, Yanagida T, Sako Y. 2006. Single-molecule analysis of epidermal growth factor binding on the surface of living cells. The EMBO Journal 25:4215-4222. doi: 10.1038/sj.emboj. 7601308
    • (2006) The EMBO Journal , vol.25 , pp. 4215-4222
    • Teramura, Y.1    Ichinose, J.2    Takagi, H.3    Nishida, K.4    Yanagida, T.5    Sako, Y.6
  • 50
    • 84933516708 scopus 로고    scopus 로고
    • SH2-PLA: A sensitive in-solution approach for quantification of modular domain binding by proximity ligation and real-time PCR
    • Thompson CM, Bloom LR, Ogiue-Ikeda M, Machida K. 2015. SH2-PLA: a sensitive in-solution approach for quantification of modular domain binding by proximity ligation and real-time PCR. BMC Biotechnology 15. doi:10.1186/s12896-015-0169-1
    • (2015) BMC Biotechnology , pp. 15
    • Thompson, C.M.1    Bloom, L.R.2    Ogiue-Ikeda, M.3    Machida, K.4
  • 52
    • 33745622868 scopus 로고    scopus 로고
    • Two Sample Logo: A graphical representation of the differences between two sets of sequence alignments
    • Vacic V, Iakoucheva LM, Radivojac P. 2006. Two Sample Logo: a graphical representation of the differences between two sets of sequence alignments. Bioinformatics 22:1536-1537. doi: 10.1093/bioinformatics/btl151
    • (2006) Bioinformatics , vol.22 , pp. 1536-1537
    • Vacic, V.1    Iakoucheva, L.M.2    Radivojac, P.3
  • 53
    • 54049146208 scopus 로고    scopus 로고
    • Quantitative microscopy and systems biology: Seeing the whole picture
    • Verveer PJ, Bastiaens PI. 2008. Quantitative microscopy and systems biology: seeing the whole picture. Histochemistry and Cell Biology 130:833-843. doi: 10.1007/s00418-008-0517-5
    • (2008) Histochemistry and Cell Biology , vol.130 , pp. 833-843
    • Verveer, P.J.1    Bastiaens, P.I.2
  • 54
    • 84883826376 scopus 로고    scopus 로고
    • Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling
    • Wagner MJ, Stacey MM, Liu BA, Pawson T. 2013. Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling. Cold Spring Harbor Perspectives in Biology 5:a008987-19. doi:10.1101/cshperspect.a008987
    • (2013) Cold Spring Harbor Perspectives in Biology , vol.5
    • Wagner, M.J.1    Stacey, M.M.2    Liu, B.A.3    Pawson, T.4
  • 55
    • 0025240654 scopus 로고
    • Rate constants for binding, dissociation, and internalization of EGF: Effect of receptor occupancy and ligand concentration
    • Waters CM, Oberg KC, Carpenter G, Overholser KA. 1990. Rate constants for binding, dissociation, and internalization of EGF: effect of receptor occupancy and ligand concentration. Biochemistry 29:3563-3569. doi:10.1021/bi00466a020
    • (1990) Biochemistry , vol.29 , pp. 3563-3569
    • Waters, C.M.1    Oberg, K.C.2    Carpenter, G.3    Overholser, K.A.4
  • 56
    • 0023677140 scopus 로고
    • Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system
    • Wiley HS. 1988. Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system. The Journal of Cell Biology 107:801-810. doi: 10.1083/ jcb.107.2.801
    • (1988) The Journal of Cell Biology , vol.107 , pp. 801-810
    • Wiley, H.S.1
  • 57
    • 0018726623 scopus 로고
    • Identification of epidermal growth factor receptors in a hyperproducing human epidermoid carcinoma cell line
    • Wrann MM, Fox CF. 1979. Identification of epidermal growth factor receptors in a hyperproducing human epidermoid carcinoma cell line. The Journal of Biological Chemistry 254:8083-8086.
    • (1979) The Journal of Biological Chemistry , vol.254 , pp. 8083-8086
    • Wrann, M.M.1    Fox, C.F.2
  • 58
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM. 2005. Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Molecular & Cellular Proteomics 4:1240-1250. doi: 10.1074/mcp.M500089-MCP200
    • (2005) Molecular & Cellular 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.