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Volumn 109, Issue 35, 2012, Pages 14024-14029

Fast rebinding increases dwell time of Src homology 2 (SH2)-containing proteins near the plasma membrane

Author keywords

Diffusion limited dissociation; Epidermal growth factor receptor; Reaction

Indexed keywords

PHOSPHOTYROSINE; PROTEIN SH2; PROTEIN TYROSINE KINASE;

EID: 84865560488     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1203397109     Document Type: Article
Times cited : (54)

References (31)
  • 1
    • 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
  • 2
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling
    • Liu BA, et al. (2006) The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Mol Cell 22:851-868.
    • (2006) Mol Cell , vol.22 , pp. 851-868
    • Liu, B.A.1
  • 3
    • 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.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 4
    • 12844283323 scopus 로고    scopus 로고
    • The SH2 domain: Versatile signaling module and pharmaceutical target
    • DOI 10.1016/j.bbapap.2004.10.005, PII S1570963904002882
    • Machida K, Mayer BJ (2005) The SH2 domain: Versatile signaling module and pharmaceutical target. BBA. Proteins and Proteomics 1747(1):1-25. (Pubitemid 40170450)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1747 , Issue.1 , pp. 1-25
    • Machida, K.1    Mayer, B.J.2
  • 5
    • 0042203565 scopus 로고    scopus 로고
    • SH2 and PTB domains in tyrosine kinase signaling
    • Schlessinger J, Lemmon MA (2003) SH2 and PTB domains in tyrosine kinase signaling. Sci STKE 2003:RE12.
    • (2003) Sci STKE , vol.2003
    • Schlessinger, J.1    Lemmon, M.A.2
  • 6
    • 63749086305 scopus 로고    scopus 로고
    • ErbB receptors and signaling pathways in cancer
    • Hynes NE, MacDonald G (2009) ErbB receptors and signaling pathways in cancer. Curr Opin Cell Biol 21:177-184.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 177-184
    • Hynes, N.E.1    MacDonald, G.2
  • 7
    • 10944257339 scopus 로고    scopus 로고
    • Profiling the global tyrosine phosphorylation state
    • Machida K, Mayer BJ, Nollau P (2003) Profiling the global tyrosine phosphorylation state. Mol Cell Proteomics 2:215-233.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 215-233
    • Machida, K.1    Mayer, B.J.2    Nollau, P.3
  • 8
    • 34250641161 scopus 로고    scopus 로고
    • High-throughput phosphotyrosine profiling using SH2 domains
    • Machida K, et al. (2007) High-throughput phosphotyrosine profiling using SH2 domains. Mol Cell 26:899- 915.
    • (2007) Mol Cell , vol.26 , pp. 899-915
    • Machida, K.1
  • 9
    • 33748573639 scopus 로고    scopus 로고
    • Charging it up: global analysis of protein phosphorylation
    • DOI 10.1016/j.tig.2006.08.005, PII S0168952506002630
    • Ptacek J, Snyder M (2006) Charging it up: Global analysis of protein phosphorylation. Trends Genet 22:545-554. (Pubitemid 44374129)
    • (2006) Trends in Genetics , vol.22 , Issue.10 , pp. 545-554
    • Ptacek, J.1    Snyder, M.2
  • 10
    • 55849118087 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics by mass spectrometry: Past, present, and future
    • Nita-Lazar A, Saito-Benz H, White FM (2008) Quantitative phosphoproteomics by mass spectrometry: Past, present, and future. Proteomics 8:4433-4443.
    • (2008) Proteomics , vol.8 , pp. 4433-4443
    • Nita-Lazar, A.1    Saito-Benz, H.2    White, F.M.3
  • 11
    • 49549116189 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of signaling network dynamics
    • White FM (2008) Quantitative phosphoproteomic analysis of signaling network dynamics. Curr Opin Biotechnol 19:404-409.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 404-409
    • White, F.M.1
  • 12
    • 43949125837 scopus 로고    scopus 로고
    • A quantitative study of the recruitment potential of all intracellular tyrosine residues on EGFR, FGFR1 and IGF1R
    • DOI 10.1039/b801018h
    • Kaushansky A, Gordus A, Chang B, Rush J, MacBeath G (2008) A quantitative study of the recruitment potential of all intracellular tyrosine residues on EGFR, FGFR1 and IGF1R. Mol Biosyst 4:643-653. (Pubitemid 351706308)
    • (2008) Molecular BioSystems , vol.4 , Issue.6 , pp. 643-653
    • Kaushansky, A.1    Gordus, A.2    Chang, B.3    Rush, J.4    MacBeath, G.5
  • 13
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • DOI 10.1038/nature04177, PII NATURE04177
    • 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. (Pubitemid 43083134)
    • (2006) Nature , vol.439 , Issue.7073 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 14
    • 50349088658 scopus 로고    scopus 로고
    • Investigating intracellular dynamics of FtsZ cytoskeleton with photoactivation single-molecule tracking
    • Niu L, Yu J (2008) Investigating intracellular dynamics of FtsZ cytoskeleton with photoactivation single-molecule tracking. Biophys J 95(4):2009-2016.
    • (2008) Biophys J , vol.95 , Issue.4 , pp. 2009-2016
    • Niu, L.1    Yu, J.2
  • 16
    • 31344462329 scopus 로고    scopus 로고
    • Understanding mortality rate deceleration and heterogeneity
    • Steinsaltz DR, Wachter KW (2006) Understanding mortality rate deceleration and heterogeneity. Math Popul Stud 13:19-37.
    • (2006) Math Popul Stud , vol.13 , pp. 19-37
    • Steinsaltz, D.R.1    Wachter, K.W.2
  • 17
    • 2942733237 scopus 로고    scopus 로고
    • Changes in structural dynamics of the Grb2 adaptor protein upon binding of phosphotyrosine ligand to its SH2 domain
    • de Mol NJ, et al. (2004) Changes in structural dynamics of the Grb2 adaptor protein upon binding of phosphotyrosine ligand to its SH2 domain. BBA. Proteins and Proteomics 1700:53-64.
    • (2004) BBA. Proteins and Proteomics , vol.1700 , pp. 53-64
    • De Mol, N.J.1
  • 21
    • 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. Biophys J 74:1215-1228. (Pubitemid 28108532)
    • (1998) Biophysical Journal , vol.74 , Issue.3 , pp. 1215-1228
    • Lagerholm, B.C.1    Thompson, N.L.2
  • 22
    • 0034077947 scopus 로고    scopus 로고
    • Translational diffusion of globular proteins in the cytoplasm of cultured muscle cells
    • Arrio-DupontM, Foucault G, Vacher M, Devaux PF, Cribier S (2000) Translational diffusion of globular proteins in the cytoplasm of cultured muscle cells. Biophys J 78:901-907. (Pubitemid 30211847)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 901-907
    • Arrio-Dupont, M.1    Foucault, G.2    Vacher, M.3    Devaux, P.F.4    Cribier, S.5
  • 23
    • 23244442694 scopus 로고    scopus 로고
    • Cholesterol dictates the freedom of EGF receptors and HER2 in the plane of the membrane
    • DOI 10.1529/biophysj.104.056192
    • Orr G, et al. (2005) Cholesterol dictates the freedom of EGF receptors and HER2 in the plane of the membrane. Biophys J 89:1362-1373. (Pubitemid 41099018)
    • (2005) Biophysical Journal , vol.89 , Issue.2 , pp. 1362-1373
    • Orr, G.1    Hu, D.2    Ozcelik, S.3    Opresko, L.K.4    Wiley, H.S.5    Colson, S.D.6
  • 25
    • 0000374718 scopus 로고    scopus 로고
    • The Grb2-mSos1 complex binds phosphopeptides with higher affinity than Grb2
    • DOI 10.1074/jbc.271.48.30472
    • Chook YM, Gish GD, Kay CM, Pai EF, Pawson T (1996) The Grb2-mSos1 complex binds phosphopeptides with higher af finity than Grb2. J Biol Chem 271:30472-30478. (Pubitemid 26404053)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.48 , pp. 30472-30478
    • Chook, Y.M.1
  • 26
    • 80052211582 scopus 로고    scopus 로고
    • Rapid phospho-turnover by receptor tyrosine kinases impacts downstream signaling and drug binding
    • Kleiman LB, Maiwald T, Conzelmann H, Lauffenburger DA, Sorger PK (2011) Rapid phospho-turnover by receptor tyrosine kinases impacts downstream signaling and drug binding. Mol Cell 43:723-737.
    • (2011) Mol Cell , vol.43 , pp. 723-737
    • Kleiman, L.B.1    Maiwald, T.2    Conzelmann, H.3    Lauffenburger, D.A.4    Sorger, P.K.5
  • 27
    • 56649112976 scopus 로고    scopus 로고
    • Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor
    • Mittag T, et al. (2008) Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. Proc Natl Acad Sci USA 105:17772-17777.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17772-17777
    • Mittag, T.1
  • 28
    • 0027211693 scopus 로고
    • Phospholipase C-gamma1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal
    • DOI 10.1016/0092-8674(93)90232-F
    • Valius M, Kazlauskas A (1993) Phospholipase C-gamma 1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal. Cell 73:321-334. (Pubitemid 23123310)
    • (1993) Cell , vol.73 , Issue.2 , pp. 321-334
    • Valius, M.1    Kazlauskas, A.2
  • 29
    • 0030794283 scopus 로고    scopus 로고
    • Distinct tyrosine autophosphorylation sites negatively and positively modulate neu-mediated transformation
    • Dankort DL, Wang Z, Blackmore V, Moran MF, Muller WJ (1997) Distinct tyrosine autophosphorylation sites negatively and positively modulate neu-mediated transformation. Mol Cell Biol 17:5410-5425. (Pubitemid 27357639)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.9 , pp. 5410-5425
    • Dankort, D.L.1    Wang, Z.2    Blackmore, V.3    Moran, M.F.4    Muller, W.J.5
  • 30
    • 84863243912 scopus 로고    scopus 로고
    • Membrane clustering and the role of rebinding in biochemical signaling
    • Mugler A, Bailey AG, Takahashi K, ten Wolde PR (2012) Membrane clustering and the role of rebinding in biochemical signaling. Biophys J 102:1069-1078.
    • (2012) Biophys J , vol.102 , pp. 1069-1078
    • Mugler, A.1    Bailey, A.G.2    Takahashi, K.3    Ten Wolde, P.R.4
  • 31
    • 0029063148 scopus 로고
    • Kinetic proofreading in T-cell receptor signal transduction
    • McKeithan TW (1995) Kinetic proofreading in T-cell receptor signal transduction. Proc Natl Acad Sci USA 92:5042-5046.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5042-5046
    • McKeithan, T.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.