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Volumn 230, Issue 1, 2004, Pages 119-132

On the cross-regulation of protein tyrosine phosphatases and receptor tyrosine kinases in intracellular signaling

Author keywords

Kinase; Phosphatase; Phosphorylation; Receptor; Signal transduction

Indexed keywords

PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE SHP 2;

EID: 3242722271     PISSN: 00225193     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jtbi.2004.04.023     Document Type: Article
Times cited : (13)

References (49)
  • 1
    • 0142059890 scopus 로고    scopus 로고
    • Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling
    • Agazie Y.M., Hayman M.J. Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling. Mol. Cell. Biol. 23:2003;7875-7886
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7875-7886
    • Agazie, Y.M.1    Hayman, M.J.2
  • 2
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • Bhalla U.S., Iyengar R. Emergent properties of networks of biological signaling pathways. Science. 283:1999;381-387
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 3
    • 0034731372 scopus 로고    scopus 로고
    • Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines
    • Bjorge J.D., Pang A., Fujita D.J. Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines. J. Biol. Chem. 275:2000;41439-41446
    • (2000) J. Biol. Chem. , vol.275 , pp. 41439-41446
    • Bjorge, J.D.1    Pang, A.2    Fujita, D.J.3
  • 4
    • 0032864252 scopus 로고    scopus 로고
    • Spatial gradients of cellular phospho-proteins
    • Brown G.C., Kholodenko B.N. Spatial gradients of cellular phospho-proteins. FEBS Lett. 457:1999;452-454
    • (1999) FEBS Lett. , vol.457 , pp. 452-454
    • Brown, G.C.1    Kholodenko, B.N.2
  • 5
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown M.T., Cooper J.A. Regulation, substrates and functions of src. Biochim. Biophys. Acta. 1287:1996;121-149
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 7
    • 0037020233 scopus 로고    scopus 로고
    • Insight into the role of low molecular weight phosphotyrosine phosphatase (LMW-PTP) on platelet-derived growth factor receptor (PDGF-r) signaling: LMW-PTP controls PDGF-r kinase activity through Tyr-857 dephosphorylation
    • Chiarugi P., Cirri P., Taddei M.L., Giannoni E., Fiaschi T., Buricchi F., Camici G., Raugei G., Ramponi G. Insight into the role of low molecular weight phosphotyrosine phosphatase (LMW-PTP) on platelet-derived growth factor receptor (PDGF-r) signaling. LMW-PTP controls PDGF-r kinase activity through Tyr-857 dephosphorylation J. Biol. Chem. 277:2002;37331-37338
    • (2002) J. Biol. Chem. , vol.277 , pp. 37331-37338
    • Chiarugi, P.1    Cirri, P.2    Taddei, M.L.3    Giannoni, E.4    Fiaschi, T.5    Buricchi, F.6    Camici, G.7    Raugei, G.8    Ramponi, G.9
  • 9
    • 0037075815 scopus 로고    scopus 로고
    • SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF β-receptor
    • Ekman S., Kallin A., Engström A., Heldin C.H. SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF β-receptor. Oncogene. 21:2002;1870-1875
    • (2002) Oncogene , vol.21 , pp. 1870-1875
    • Ekman, S.1    Kallin, A.2    Engström, A.3    Heldin, C.H.4
  • 11
    • 0027531637 scopus 로고
    • SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases
    • Feng G., Hui C., Pawson T. SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases. Science. 259:1993;1607-1610
    • (1993) Science , vol.259 , pp. 1607-1610
    • Feng, G.1    Hui, C.2    Pawson, T.3
  • 12
    • 0033598161 scopus 로고    scopus 로고
    • Intracellular movement of green fluorescent protein-tagged phosphatidylinositol 3-kinase in response to growth factor receptor signaling
    • Gillham H., Golding M.C.H.M., Pepperkok R., Gullick W.J. Intracellular movement of green fluorescent protein-tagged phosphatidylinositol 3-kinase in response to growth factor receptor signaling. J. Cell Biol. 146:1999;869-880
    • (1999) J. Cell Biol. , vol.146 , pp. 869-880
    • Gillham, H.1    Golding, M.C.H.M.2    Pepperkok, R.3    Gullick, W.J.4
  • 13
    • 0001424903 scopus 로고
    • An amplified sensitivity arising from covalent modification in biological systems
    • Goldbeter A., Koshland D.E.J. An amplified sensitivity arising from covalent modification in biological systems. Proc. Natl Acad. Sci. USA. 78:1981;6840-6844
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 6840-6844
    • Goldbeter, A.1    Koshland, D.E.J.2
  • 14
    • 0030998039 scopus 로고    scopus 로고
    • Physical modulation of intracellular signaling processes by locational regulation
    • Haugh J.M., Lauffenburger D.A. Physical modulation of intracellular signaling processes by locational regulation. Biophys. J. 72:1997;2014-2031
    • (1997) Biophys. J. , vol.72 , pp. 2014-2031
    • Haugh, J.M.1    Lauffenburger, D.A.2
  • 15
    • 0032556454 scopus 로고    scopus 로고
    • Analysis of receptor internalization as a mechanism for modulating signal transduction
    • Haugh J.M., Lauffenburger D.A. Analysis of receptor internalization as a mechanism for modulating signal transduction. J. Theor. Biol. 195:1998;187-218
    • (1998) J. Theor. Biol. , vol.195 , pp. 187-218
    • Haugh, J.M.1    Lauffenburger, D.A.2
  • 16
    • 0037081644 scopus 로고    scopus 로고
    • 2 in endosomes: Implications for phospholipase C and PI 3-kinase signaling
    • 2 in endosomes. implications for phospholipase C and PI 3-kinase signaling J. Cell Sci. 115:2002;303-310
    • (2002) J. Cell Sci. , vol.115 , pp. 303-310
    • Haugh, J.M.1    Meyer, T.2
  • 18
    • 0036285634 scopus 로고    scopus 로고
    • Mathematical models of protein kinase signal transduction
    • Heinrich R., Neel B.G., Rapoport T.A. Mathematical models of protein kinase signal transduction. Mol. Cell. 9:2002;957-970
    • (2002) Mol. Cell , vol.9 , pp. 957-970
    • Heinrich, R.1    Neel, B.G.2    Rapoport, T.A.3
  • 19
    • 0033570090 scopus 로고    scopus 로고
    • Quantification of short term signaling by the epidermal growth factor receptor
    • Kholodenko B.N., Demin O.V., Moehren G., Hoek J.B. Quantification of short term signaling by the epidermal growth factor receptor. J. Biol. Chem. 274:1999;30169-30181
    • (1999) J. Biol. Chem. , vol.274 , pp. 30169-30181
    • Kholodenko, B.N.1    Demin, O.V.2    Moehren, G.3    Hoek, J.B.4
  • 20
    • 0034194467 scopus 로고    scopus 로고
    • Why cytoplasmic signalling proteins should be recruited to cell membranes
    • Kholodenko B.N., Hoek J.B., Westerhoff H.V. Why cytoplasmic signalling proteins should be recruited to cell membranes. Trends Cell Biol. 10:2000;173-178
    • (2000) Trends Cell Biol. , vol.10 , pp. 173-178
    • Kholodenko, B.N.1    Hoek, J.B.2    Westerhoff, H.V.3
  • 21
    • 0029085194 scopus 로고
    • Identification of a putative Syp substrate, the PDGFβ receptor
    • Klinghoffer R.A., Kazlauskas A. Identification of a putative Syp substrate, the PDGFβ receptor. J. Biol. Chem. 270:1995;22208-22217
    • (1995) J. Biol. Chem. , vol.270 , pp. 22208-22217
    • Klinghoffer, R.A.1    Kazlauskas, A.2
  • 22
    • 0034717163 scopus 로고    scopus 로고
    • Site-selective dephosphorylation of the platelet-derived growth factor β-receptor by the receptor-like protein-tyrosine phosphatase DEP-1
    • Kovalenko M., Denner K., Sandström J., Persson C., Groß S., Jandt E., Vilella R., Böhmer F., Östman A. Site-selective dephosphorylation of the platelet-derived growth factor β-receptor by the receptor-like protein-tyrosine phosphatase DEP-1. J. Biol. Chem. 275:2000;16219-16226
    • (2000) J. Biol. Chem. , vol.275 , pp. 16219-16226
    • Kovalenko, M.1    Denner, K.2    Sandström, J.3    Persson, C.4    Groß, S.5    Jandt, E.6    Vilella, R.7    Böhmer, F.8    Östman, A.9
  • 24
    • 0027432407 scopus 로고
    • Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor
    • Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor. J. Biol. Chem. 268:1993;21478-21481
    • (1993) J. Biol. Chem. , vol.268 , pp. 21478-21481
    • Lechleider, R.J.1    Sugimoto, S.2    Bennett, A.M.3    Kashishian, A.S.4    Cooper, J.A.5    Shoelson, S.E.6    Walsh, C.T.7    Neel, B.G.8
  • 25
    • 0034705227 scopus 로고    scopus 로고
    • Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties
    • Levchenko A., Bruck J., Sternberg P.W. Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties. Proc. Natl Acad. Sci. USA. 97:2000;5818-5823
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5818-5823
    • Levchenko, A.1    Bruck, J.2    Sternberg, P.W.3
  • 27
    • 0242585485 scopus 로고    scopus 로고
    • Identification of protein tyrosine phosphatases associating with the PDGF receptor
    • Markova B., Herrlich P., Rönnstrand L., Böhmer F.D. Identification of protein tyrosine phosphatases associating with the PDGF receptor. Biochemistry. 42:2003;2691-2699
    • (2003) Biochemistry , vol.42 , pp. 2691-2699
    • Markova, B.1    Herrlich, P.2    Rönnstrand, L.3    Böhmer, F.D.4
  • 28
    • 0035972164 scopus 로고    scopus 로고
    • Real time fluorescence imaging of PLCγ translocation and its interaction with the epidermal growth factor receptor
    • Matsuda M., Paterson H.F., Rodriguez R., Fensome A.C., Ellis M.V., Swann K., Katan M. Real time fluorescence imaging of PLCγ translocation and its interaction with the epidermal growth factor receptor. J. Cell Biol. 153:2001;599-612
    • (2001) J. Cell Biol. , vol.153 , pp. 599-612
    • Matsuda, M.1    Paterson, H.F.2    Rodriguez, R.3    Fensome, A.C.4    Ellis, M.V.5    Swann, K.6    Katan, M.7
  • 29
    • 0038771965 scopus 로고    scopus 로고
    • The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
    • Neel B.G., Gu H.H., Pao L. The 'Shp'ing news. SH2 domain-containing tyrosine phosphatases in cell signaling Trends Biochem. Sci. 28:2003;284-293
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 284-293
    • Neel, B.G.1    Gu, H.H.2    Pao, L.3
  • 30
    • 0035371620 scopus 로고    scopus 로고
    • Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases
    • Östman A., Böhmer F.D. Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases. Trends Cell Biol. 11:2001;258-266
    • (2001) Trends Cell Biol. , vol.11 , pp. 258-266
    • Östman, A.1    Böhmer, F.D.2
  • 31
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • Pawson T., Gish G.D., 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
  • 32
    • 0028837693 scopus 로고
    • Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association
    • Peng Z.Y., Cartwright C.A. Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association. Oncogene. 11:1995;1955-1962
    • (1995) Oncogene , vol.11 , pp. 1955-1962
    • Peng, Z.Y.1    Cartwright, C.A.2
  • 34
    • 0033600129 scopus 로고    scopus 로고
    • SHP-2 binds to Tyr763 and Tyr1009 in the PDGF beta-receptor and mediates PDGF-induced activation of the Ras MAP kinase pathway and chemotaxis
    • Rönnstrand L., Arvidsson A.K., Kallin A., Rorsman C., Hellman U., Engstrom U., Wernstedt C., Heldin C.H. SHP-2 binds to Tyr763 and Tyr1009 in the PDGF beta-receptor and mediates PDGF-induced activation of the Ras MAP kinase pathway and chemotaxis. Oncogene. 18:1999;3696-3702
    • (1999) Oncogene , vol.18 , pp. 3696-3702
    • Rönnstrand, L.1    Arvidsson, A.K.2    Kallin, A.3    Rorsman, C.4    Hellman, U.5    Engstrom, U.6    Wernstedt, C.7    Heldin, C.H.8
  • 35
    • 0026567491 scopus 로고
    • SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: Identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase Cγ
    • Rotin D., Margolis B., Mohammadi M., Daly R.J., Daum G., Li N., Fischer E.H., Burgess W.H., Ullrich A., Schlessinger J. SH2 domains prevent tyrosine dephosphorylation of the EGF receptor. identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase Cγ EMBO J. 11:1992;559-567
    • (1992) EMBO J. , vol.11 , pp. 559-567
    • Rotin, D.1    Margolis, B.2    Mohammadi, M.3    Daly, R.J.4    Daum, G.5    Li, N.6    Fischer, E.H.7    Burgess, W.H.8    Ullrich, A.9    Schlessinger, J.10
  • 36
    • 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
  • 37
    • 0028277954 scopus 로고
    • Individual epidermal growth factor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins
    • Soler C., Beguinot L., Carpenter G. Individual epidermal growth factor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins. J. Biol. Chem. 269:1994;12320-12324
    • (1994) J. Biol. Chem. , vol.269 , pp. 12320-12324
    • Soler, C.1    Beguinot, L.2    Carpenter, G.3
  • 38
    • 0034597554 scopus 로고    scopus 로고
    • Interaction of EGF receptor and Grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy
    • Sorkin A., McClure M., Huang F.T., Carter R. Interaction of EGF receptor and Grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy. Curr. Biol. 10:2000;1395-1398
    • (2000) Curr. Biol. , vol.10 , pp. 1395-1398
    • Sorkin, A.1    McClure, M.2    Huang, F.T.3    Carter, R.4
  • 39
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized IgE receptor-mediated signal transduction in living cells
    • Stauffer T.P., Meyer T. Compartmentalized IgE receptor-mediated signal transduction in living cells. J. Cell Biol. 139:1997;1447-1454
    • (1997) J. Cell Biol. , vol.139 , pp. 1447-1454
    • Stauffer, T.P.1    Meyer, T.2
  • 40
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas S.M., Brugge J.S. Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 13:1997;513-609
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 41
    • 0035313868 scopus 로고    scopus 로고
    • Combinatorial control of the specificity of protein tyrosine phosphatases
    • Tonks N.K., Neel B.G. Combinatorial control of the specificity of protein tyrosine phosphatases. Curr. Opin. Cell Biol. 13:2001;182-195
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 182-195
    • Tonks, N.K.1    Neel, B.G.2
  • 42
    • 0028170817 scopus 로고
    • Receptor protein-tyrosine kinases and their signal transduction pathways
    • van der Geer P., Hunter T., Lindberg R.A. Receptor protein-tyrosine kinases and their signal transduction pathways. Annu. Rev. Cell Biol. 10:1994;251-337
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 251-337
    • Van Der Geer, P.1    Hunter, T.2    Lindberg, R.A.3
  • 43
    • 0027399168 scopus 로고
    • Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation
    • Vogel W., Lammers R., Huang J., Ullrich A. Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation. Science. 259:1993;1611-1614
    • (1993) Science , vol.259 , pp. 1611-1614
    • Vogel, W.1    Lammers, R.2    Huang, J.3    Ullrich, A.4
  • 44
    • 0035399162 scopus 로고    scopus 로고
    • EGF-dependent translocation of green fluorescent protein-tagged PLC-γ1 to the plasma membrane and endosomes
    • Wang X.J., Liao H.J., Chattopadhyay A., Carpenter G. EGF-dependent translocation of green fluorescent protein-tagged PLC-γ1 to the plasma membrane and endosomes. Exp. Cell Res. 267:2001;28-36
    • (2001) Exp. Cell Res. , vol.267 , pp. 28-36
    • Wang, X.J.1    Liao, H.J.2    Chattopadhyay, A.3    Carpenter, G.4
  • 45
    • 0031573523 scopus 로고    scopus 로고
    • Exploiting the difference between intrinsic and extrinsic kinases: Implications for regulation of signaling by immunoreceptors
    • Wofsy C., Torigoe C., Kent U.M., Metzger H., Goldstein B. Exploiting the difference between intrinsic and extrinsic kinases. implications for regulation of signaling by immunoreceptors J. Immunol. 159:1997;5984-5992
    • (1997) J. Immunol. , vol.159 , pp. 5984-5992
    • Wofsy, C.1    Torigoe, C.2    Kent, U.M.3    Metzger, H.4    Goldstein, B.5
  • 46
    • 0033587769 scopus 로고    scopus 로고
    • One Lyn molecule is sufficient to initiate phosphorylation of aggregated high-affinity IgE receptors
    • Wofsy C., Vonakis B.M., Metzger H., Goldstein B. One Lyn molecule is sufficient to initiate phosphorylation of aggregated high-affinity IgE receptors. Proc. Natl Acad. Sci. USA. 96:1999;8615-8620
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8615-8620
    • Wofsy, C.1    Vonakis, B.M.2    Metzger, H.3    Goldstein, B.4
  • 47
    • 0032488828 scopus 로고    scopus 로고
    • SHP-1 associates with both platelet-derived growth factor receptor and the p85 subunit of phosphatidylinositol 3-kinase
    • Yu Z., Su L., Hoglinger O., Jaramillo M.L., Banville D., Shen S. SHP-1 associates with both platelet-derived growth factor receptor and the p85 subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 273:1998;3687-3694
    • (1998) J. Biol. Chem. , vol.273 , pp. 3687-3694
    • Yu, Z.1    Su, L.2    Hoglinger, O.3    Jaramillo, M.L.4    Banville, D.5    Shen, S.6
  • 48
    • 0037737741 scopus 로고    scopus 로고
    • The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation
    • Zhang Z.S., Shen K Lu W., Cole P.A. The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation. J. Biol. Chem. 278:2003;4668-4674
    • (2003) J. Biol. Chem. , vol.278 , pp. 4668-4674
    • Zhang, Z.S.1    Shen, K.L.W.2    Cole, P.A.3
  • 49
    • 0033558225 scopus 로고    scopus 로고
    • Tyrosine phosphatase SHP-2 dephosphorylates the platelet-derived growth factor receptor but enhances its downstream signalling
    • Zhao R., Zhao Z.J. Tyrosine phosphatase SHP-2 dephosphorylates the platelet-derived growth factor receptor but enhances its downstream signalling. Biochem. J. 338:1999;35-39
    • (1999) Biochem. J. , vol.338 , pp. 35-39
    • Zhao, R.1    Zhao, Z.J.2


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