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Volumn 288, Issue 32, 2013, Pages 23421-23431

Substrate specificity of R3 receptor-like protein-tyrosine phosphatase subfamily toward receptor protein-tyrosine kinases

Author keywords

[No Author keywords available]

Indexed keywords

PHYSIOLOGICAL ROLES; PROTEIN-TYROSINE KINASE; PROTEIN-TYROSINE PHOSPHATASE; SUBSTRATE SPECIFICITY;

EID: 84881426238     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.458489     Document Type: Article
Times cited : (13)

References (42)
  • 1
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen, P., and Hunter, T. (2001) Oncogenic kinase signalling. Nature 411, 355-365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 2
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard, S. R., and Till, J. H. (2000) Protein tyrosine kinase structure and function. Annu. Rev. Biochem. 69, 373-398
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 5
    • 79959351734 scopus 로고    scopus 로고
    • Expression, localization, and biological function of the R3 subtype of receptor-type protein tyrosine phosphatases in mammals
    • Matozaki, T., Murata, Y., Mori, M., Kotani, T., Okazawa, H., and Ohnishi, H. (2010) Expression, localization, and biological function of the R3 subtype of receptor-type protein tyrosine phosphatases in mammals. Cell. Signal. 22, 1811-1817
    • (2010) Cell. Signal. , vol.22 , pp. 1811-1817
    • Matozaki, T.1    Murata, Y.2    Mori, M.3    Kotani, T.4    Okazawa, H.5    Ohnishi, H.6
  • 6
    • 33745698914 scopus 로고    scopus 로고
    • Eph receptors are negatively controlled by protein tyrosine phosphatase receptor type O
    • Shintani, T., Ihara, M., Sakuta, H., Takahashi, H., Watakabe, I., and Noda, M. (2006) Eph receptors are negatively controlled by protein tyrosine phosphatase receptor type O. Nat. Neurosci. 9, 761-769
    • (2006) Nat. Neurosci. , vol.9 , pp. 761-769
    • Shintani, T.1    Ihara, M.2    Sakuta, H.3    Takahashi, H.4    Watakabe, I.5    Noda, M.6
  • 7
    • 36849063719 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of ErbB4 is enhanced by PSD95 and repressed by protein tyrosine phosphatase receptor type Z
    • Fujikawa, A., Chow, J. P., Shimizu, H., Fukada, M., Suzuki, R., and Noda, M. (2007) Tyrosine phosphorylation of ErbB4 is enhanced by PSD95 and repressed by protein tyrosine phosphatase receptor type Z. J. Biochem. 142, 343-350
    • (2007) J. Biochem. , vol.142 , pp. 343-350
    • Fujikawa, A.1    Chow, J.P.2    Shimizu, H.3    Fukada, M.4    Suzuki, R.5    Noda, M.6
  • 8
    • 48749118176 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase receptor type Z dephosphorylates TrkA receptors and attenuates NGF-dependent neurite outgrowth of PC12 cells
    • Shintani, T., and Noda, M. (2008) Protein tyrosine phosphatase receptor type Z dephosphorylates TrkA receptors and attenuates NGF-dependent neurite outgrowth of PC12 cells. J. Biochem. 144, 259-266
    • (2008) J. Biochem. , vol.144 , pp. 259-266
    • Shintani, T.1    Noda, M.2
  • 9
    • 0031055324 scopus 로고    scopus 로고
    • Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases
    • Flint, A. J., Tiganis, T., Barford, D., and Tonks, N. K. (1997) Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases. Proc. Natl. Acad. Sci. U.S.A. 94, 1680-1685
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 10
    • 0038272006 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase RQ is a phosphatidylinositol phosphatase that can regulate cell survival and proliferation
    • Oganesian, A., Poot, M., Daum, G., Coats, S. A., Wright, M. B., Seifert, R. A., and Bowen-Pope, D. F. (2003) Protein tyrosine phosphatase RQ is a phosphatidylinositol phosphatase that can regulate cell survival and proliferation. Proc. Natl. Acad. Sci. U.S.A. 100, 7563-7568
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 7563-7568
    • Oganesian, A.1    Poot, M.2    Daum, G.3    Coats, S.A.4    Wright, M.B.5    Seifert, R.A.6    Bowen-Pope, D.F.7
  • 11
    • 84869170890 scopus 로고    scopus 로고
    • Receptor-type protein tyrosine phosphatase regulates Met phosphorylation and function in head and neck squamous cell carcinoma
    • Xu, Y., Zhou, J., Carey, T. E., McHugh, J. B., Voorhees, J. J., and Fisher, G. J. (2012) Receptor-type protein tyrosine phosphatase regulates Met phosphorylation and function in head and neck squamous cell carcinoma. Neoplasia 14, 1015-1022
    • (2012) Neoplasia , vol.14 , pp. 1015-1022
    • Xu, Y.1    Zhou, J.2    Carey, T.E.3    McHugh, J.B.4    Voorhees, J.J.5    Fisher, G.J.6
  • 12
    • 0037458646 scopus 로고    scopus 로고
    • Hepatocyte growth factor receptor tyrosine kinase Met is a substrate of the receptor protein-tyrosine phosphatase DEP-1
    • Palka, H. L., Park, M., and Tonks, N. K. (2003) Hepatocyte growth factor receptor tyrosine kinase Met is a substrate of the receptor protein-tyrosine phosphatase DEP-1. J. Biol. Chem. 278, 5728-5735
    • (2003) J. Biol. Chem. , vol.278 , pp. 5728-5735
    • Palka, H.L.1    Park, M.2    Tonks, N.K.3
  • 13
    • 33745714241 scopus 로고    scopus 로고
    • The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins
    • Iervolino, A., Iuliano, R., Trapasso, F., Viglietto, G., Melillo, R. M., Carlomagno, F., Santoro, M., and Fusco, A. (2006) The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins. Cancer Res. 66, 6280-6287
    • (2006) Cancer Res. , vol.66 , pp. 6280-6287
    • Iervolino, A.1    Iuliano, R.2    Trapasso, F.3    Viglietto, G.4    Melillo, R.M.5    Carlomagno, F.6    Santoro, M.7    Fusco, A.8
  • 14
    • 0023473236 scopus 로고
    • Acidic and basic fibroblast growth factors promote stable neurite outgrowth and neuronal differentiation in cultures of PC12 cells
    • Rydel, R. E., and Greene, L. A. (1987) Acidic and basic fibroblast growth factors promote stable neurite outgrowth and neuronal differentiation in cultures of PC12 cells. J. Neurosci. 7, 3639-3653
    • (1987) J. Neurosci. , vol.7 , pp. 3639-3653
    • Rydel, R.E.1    Greene, L.A.2
  • 15
    • 0031806908 scopus 로고    scopus 로고
    • Identification of the cytoplasmic regions of fibroblast growth factor (FGF) receptor 1 which play important roles in induction of neurite outgrowth in PC12 cells by FGF-1
    • Lin, H. Y., Xu, J., Ischenko, I., Ornitz, D. M., Halegoua, S., and Hayman, M. J. (1998) Identification of the cytoplasmic regions of fibroblast growth factor (FGF) receptor 1 which play important roles in induction of neurite outgrowth in PC12 cells by FGF-1. Mol. Cell. Biol. 18, 3762-3770
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3762-3770
    • Lin, H.Y.1    Xu, J.2    Ischenko, I.3    Ornitz, D.M.4    Halegoua, S.5    Hayman, M.J.6
  • 16
    • 0026569297 scopus 로고
    • Activation of microtubule-associated protein kinase in PC12D cells in response to both fibroblast growth factor and epidermal growth factor and concomitant stimulation of the outgrowth of neurites
    • Sano, M., and Kitajima, S. (1992) Activation of microtubule-associated protein kinase in PC12D cells in response to both fibroblast growth factor and epidermal growth factor and concomitant stimulation of the outgrowth of neurites. J. Neurochem. 58, 837-844
    • (1992) J. Neurochem. , vol.58 , pp. 837-844
    • Sano, M.1    Kitajima, S.2
  • 17
    • 0035837429 scopus 로고    scopus 로고
    • Glial cell line-derived neurotrophic factor promotes survival and induces differentiation through the phosphatidylinositol 3-kinase and mitogenactivated protein kinase pathway respectively in PC12 cells
    • Chen, Z., Chai, Y., Cao, L., Huang, A., Cui, R., Lu, C., and He, C. (2001) Glial cell line-derived neurotrophic factor promotes survival and induces differentiation through the phosphatidylinositol 3-kinase and mitogenactivated protein kinase pathway respectively in PC12 cells. Neuroscience 104, 593-598
    • (2001) Neuroscience , vol.104 , pp. 593-598
    • Chen, Z.1    Chai, Y.2    Cao, L.3    Huang, A.4    Cui, R.5    Lu, C.6    He, C.7
  • 18
    • 0035810942 scopus 로고    scopus 로고
    • Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase/by the yeast substrate-trapping system
    • Kawachi, H., Fujikawa, A., Maeda, N., and Noda, M. (2001) Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase/by the yeast substrate-trapping system. Proc. Natl. Acad. Sci. U.S.A. 98, 6593-6598
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6593-6598
    • Kawachi, H.1    Fujikawa, A.2    Maeda, N.3    Noda, M.4
  • 20
    • 33745457190 scopus 로고    scopus 로고
    • Genetic ablation of Ptprj, a mouse cancer susceptibility gene, results in normal growth and development and does not predispose to spontaneous tumorigenesis
    • Trapasso, F., Drusco, A., Costinean, S., Alder, H., Aqeilan, R. I., Iuliano, R., Gaudio, E., Raso, C., Zanesi, N., Croce, C. M., and Fusco, A. (2006) Genetic ablation of Ptprj, a mouse cancer susceptibility gene, results in normal growth and development and does not predispose to spontaneous tumorigenesis. DNA Cell Biol. 25, 376-382
    • (2006) DNA Cell Biol. , vol.25 , pp. 376-382
    • Trapasso, F.1    Drusco, A.2    Costinean, S.3    Alder, H.4    Aqeilan, R.I.5    Iuliano, R.6    Gaudio, E.7    Raso, C.8    Zanesi, N.9    Croce, C.M.10    Fusco, A.11
  • 21
    • 70350778444 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase receptor type O regulates development and function of the sensory nervous system
    • Gonzalez-Brito, M. R., and Bixby, J. L. (2009) Protein tyrosine phosphatase receptor type O regulates development and function of the sensory nervous system. Mol. Cell. Neurosci. 42, 458-465
    • (2009) Mol. Cell. Neurosci. , vol.42 , pp. 458-465
    • Gonzalez-Brito, M.R.1    Bixby, J.L.2
  • 22
    • 0037450376 scopus 로고    scopus 로고
    • Expression of PTPRO during mouse development suggests involvement in axonogenesis and differentiation of NT-3 and NGF-dependent neurons
    • Beltran, P. J., Bixby, J. L., and Masters, B. A. (2003) Expression of PTPRO during mouse development suggests involvement in axonogenesis and differentiation of NT-3 and NGF-dependent neurons. J. Comp. Neurol. 456, 384-395
    • (2003) J. Comp. Neurol. , vol.456 , pp. 384-395
    • Beltran, P.J.1    Bixby, J.L.2    Masters, B.A.3
  • 23
    • 0033592739 scopus 로고    scopus 로고
    • Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2
    • Fachinger, G., Deutsch, U., and Risau, W. (1999) Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2. Oncogene 18, 5948-5953
    • (1999) Oncogene , vol.18 , pp. 5948-5953
    • Fachinger, G.1    Deutsch, U.2    Risau, W.3
  • 26
    • 0031559401 scopus 로고    scopus 로고
    • Unified nomenclature for Eph family receptors and their ligands, the ephrins
    • Eph Nomenclature Committee
    • Eph Nomenclature Committee (1997) Unified nomenclature for Eph family receptors and their ligands, the ephrins. Cell 90, 403-404
    • (1997) Cell , vol.90 , pp. 403-404
  • 27
    • 5044240692 scopus 로고    scopus 로고
    • Diverse roles of Eph receptors and ephrins in the regulation of cell migration and tissue assembly
    • Poliakov, A., Cotrina, M., and Wilkinson, D. G. (2004) Diverse roles of Eph receptors and ephrins in the regulation of cell migration and tissue assembly. Dev. Cell 7, 465-480
    • (2004) Dev. Cell , vol.7 , pp. 465-480
    • Poliakov, A.1    Cotrina, M.2    Wilkinson, D.G.3
  • 28
    • 41149084179 scopus 로고    scopus 로고
    • Eph-ephrin bidirectional signaling in physiology and disease
    • Pasquale, E. B. (2008) Eph-ephrin bidirectional signaling in physiology and disease. Cell 133, 38-52
    • (2008) Cell , vol.133 , pp. 38-52
    • Pasquale, E.B.1
  • 29
    • 0029789246 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase DEP-1 is induced during differentiation and inhibits growth of breast cancer cells
    • Keane, M. M., Lowrey, G. A., Ettenberg, S. A., Dayton, M. A., and Lipkowitz, S. (1996) The protein tyrosine phosphatase DEP-1 is induced during differentiation and inhibits growth of breast cancer cells. Cancer Res. 56, 4236-4243
    • (1996) Cancer Res. , vol.56 , pp. 4236-4243
    • Keane, M.M.1    Lowrey, G.A.2    Ettenberg, S.A.3    Dayton, M.A.4    Lipkowitz, S.5
  • 30
    • 0034458955 scopus 로고    scopus 로고
    • Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kip1)
    • Trapasso, F., Iuliano, R., Boccia, A., Stella, A., Visconti, R., Bruni, P., Baldassarre, G., Santoro, M., Viglietto, G., and Fusco, A. (2000) Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kip1). Mol. Cell. Biol. 20, 9236-9246
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9236-9246
    • Trapasso, F.1    Iuliano, R.2    Boccia, A.3    Stella, A.4    Visconti, R.5    Bruni, P.6    Baldassarre, G.7    Santoro, M.8    Viglietto, G.9    Fusco, A.10
  • 35
    • 42649140235 scopus 로고    scopus 로고
    • Immunobiology of the TAM receptors
    • Lemke, G., and Rothlin, C. V. (2008) Immunobiology of the TAM receptors. Nat. Rev. Immunol. 8, 327-336
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 327-336
    • Lemke, G.1    Rothlin, C.V.2
  • 36
    • 0035854442 scopus 로고    scopus 로고
    • Homeostatic regulation of the immune system by receptor tyrosine kinases of the Tyro 3 family
    • Lu, Q., and Lemke, G. (2001) Homeostatic regulation of the immune system by receptor tyrosine kinases of the Tyro 3 family. Science 293, 306-311
    • (2001) Science , vol.293 , pp. 306-311
    • Lu, Q.1    Lemke, G.2
  • 37
    • 4043107043 scopus 로고    scopus 로고
    • Regulated expression of the receptor-like tyrosine phosphatase CD148 on hemopoietic cells
    • Lin, J., Zhu, J. W., Baker, J. E., and Weiss, A. (2004) Regulated expression of the receptor-like tyrosine phosphatase CD148 on hemopoietic cells. J. Immunol. 173, 2324-2330
    • (2004) J. Immunol. , vol.173 , pp. 2324-2330
    • Lin, J.1    Zhu, J.W.2    Baker, J.E.3    Weiss, A.4
  • 38
    • 0035102841 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reducedLATand phospholipaseC1 phosphorylation
    • Baker, J. E., Majeti, R., Tangye, S. G., and Weiss, A. (2001) Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reducedLATand phospholipaseC1 phosphorylation. Mol. Cell. Biol. 21, 2393-2403
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2393-2403
    • Baker, J.E.1    Majeti, R.2    Tangye, S.G.3    Weiss, A.4
  • 40
    • 84877089860 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase receptor type O inhibits trigeminal axon growth and branching by repressing TrkB and Ret signaling
    • Gatto, G., Dudanova, I., Suetterlin, P., Davies, A. M., Drescher, U., Bixby, J. L., and Klein, R. (2013) Protein tyrosine phosphatase receptor type O inhibits trigeminal axon growth and branching by repressing TrkB and Ret signaling. J. Neurosci. 33, 5399-5410
    • (2013) J. Neurosci. , vol.33 , pp. 5399-5410
    • Gatto, G.1    Dudanova, I.2    Suetterlin, P.3    Davies, A.M.4    Drescher, U.5    Bixby, J.L.6    Klein, R.7
  • 42
    • 41949092558 scopus 로고    scopus 로고
    • Fibroblast growth factor regulation of neovascularization
    • Murakami, M., and Simons, M. (2008) Fibroblast growth factor regulation of neovascularization. Curr. Opin. Hematol. 15, 215-220
    • (2008) Curr. Opin. Hematol. , vol.15 , pp. 215-220
    • Murakami, M.1    Simons, M.2


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