메뉴 건너뛰기




Volumn 13, Issue 2, 2011, Pages 174-181

Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; EPIDERMAL GROWTH FACTOR RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOTYROSINE; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; TYROSINE; PRMT5 PROTEIN, HUMAN; PROTEIN METHYLTRANSFERASE;

EID: 79551606798     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb2158     Document Type: Article
Times cited : (189)

References (30)
  • 1
    • 0035901570 scopus 로고    scopus 로고
    • Epidermal growth factor receptor signaling
    • Bogdan, S. & Klambt, C. Epidermal growth factor receptor signaling. Curr. Biol. 11, R292-R295 (2001).
    • (2001) Curr. Biol. , vol.11
    • Bogdan, S.1    Klambt, C.2
  • 2
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • Citri, A. & Yarden, Y. EGF-ERBB signalling: towards the systems level. Nat. Rev. Mol. Cell Biol. 7, 505-516 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 3
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • Hynes, N. E. & Lane, H. A. ERBB receptors and cancer: the complexity of targeted inhibitors. Nat. Rev. Cancer 5, 341-354 (2005).
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 4
    • 33751328082 scopus 로고    scopus 로고
    • ErbB receptors: New insights on mechanisms and biology
    • Linggi, B. & Carpenter, G. ErbB receptors: new insights on mechanisms and biology. Trends Cell Biol. 16, 649-656 (2006).
    • (2006) Trends Cell Biol. , vol.16 , pp. 649-656
    • Linggi, B.1    Carpenter, G.2
  • 5
    • 33847678615 scopus 로고    scopus 로고
    • Historical review: The field of protein methylation
    • Paik, W. K., Paik, D. C. & Kim, S. Historical review: the field of protein methylation. Trends Biochem. Sci. 32, 146-152 (2007).
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 146-152
    • Paik, W.K.1    Paik, D.C.2    Kim, S.3
  • 6
    • 38349035858 scopus 로고    scopus 로고
    • Arginine methylation at a glance
    • Bedford, M. T. Arginine methylation at a glance. J. Cell Sci. 120, 4243-4246 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 4243-4246
    • Bedford, M.T.1
  • 7
    • 34250859489 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: From unicellular eukaryotes to humans
    • Bachand, F. Protein arginine methyltransferases: from unicellular eukaryotes to humans. Eukaryot. Cell 6, 889-898 (2007).
    • (2007) Eukaryot. Cell , vol.6 , pp. 889-898
    • Bachand, F.1
  • 8
    • 33845418030 scopus 로고    scopus 로고
    • Protein arginine methylation: Cellular functions and methods of analysis
    • Pahlich, S., Zakaryan, R. P. & Gehring, H. Protein arginine methylation: cellular functions and methods of analysis. Biochim. Biophys. Acta 1764, 1890-1903 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1890-1903
    • Pahlich, S.1    Zakaryan, R.P.2    Gehring, H.3
  • 9
    • 0035854372 scopus 로고    scopus 로고
    • State of the arg: Protein methylation at arginine comes of age
    • McBride, A. E. & Silver, P. A. State of the arg: protein methylation at arginine comes of age. Cell 106, 5-8 (2001).
    • (2001) Cell , vol.106 , pp. 5-8
    • McBride, A.E.1    Silver, P.A.2
  • 10
    • 0028332830 scopus 로고
    • Tyrosines 1148 and 1173 of activated human epidermal growth factor receptors are binding sites of Shc in intact cells
    • Okabayashi, Y. et al. Tyrosines 1148 and 1173 of activated human epidermal growth factor receptors are binding sites of Shc in intact cells. J. Biol. Chem. 269, 18674-18678 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18674-18678
    • Okabayashi, Y.1
  • 11
    • 0026678172 scopus 로고
    • Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
    • Rozakis-Adcock, M. et al. Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature 360, 689-692 (1992).
    • (1992) Nature , vol.360 , pp. 689-692
    • Rozakis-Adcock, M.1
  • 12
    • 0028040812 scopus 로고
    • Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor
    • Batzer, A. G., Rotin, D., Urena, J. M., Skolnik, E. Y. & Schlessinger, J. Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor. Mol. Cell Biol. 14, 5192-5201 (1994).
    • (1994) Mol. Cell Biol. , vol.14 , pp. 5192-5201
    • Batzer, A.G.1    Rotin, D.2    Urena, J.M.3    Skolnik, E.Y.4    Schlessinger, J.5
  • 13
    • 0032544418 scopus 로고    scopus 로고
    • Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling
    • Keilhack, H. et al. Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling. J. Biol. Chem. 273, 24839-24846 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 24839-24846
    • Keilhack, H.1
  • 14
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • Chang, B., Chen, Y., Zhao, Y. & Bruick, R. K. JMJD6 is a histone arginine demethylase. Science 318, 444-447 (2007).
    • (2007) Science , vol.318 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 15
    • 35848936709 scopus 로고    scopus 로고
    • Cross-regulation of histone modifications
    • Latham, J. A. & Dent, S. Y. Cross-regulation of histone modifications. Nat. Struct. Mol. Biol. 14, 1017-1024 (2007).
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1017-1024
    • Latham, J.A.1    Dent, S.Y.2
  • 16
    • 52449132322 scopus 로고    scopus 로고
    • Is there a code embedded in proteins that is based on post-translational modifications?
    • Sims, R. J. 3rd & Reinberg, D. Is there a code embedded in proteins that is based on post-translational modifications? Nat. Rev. Mol. Cell Biol. 9, 815-820 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 815-820
    • Sims Iii, R.J.1    Reinberg, D.2
  • 17
    • 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. et al. Grb2/Ash binds directly to tyrosines 1068 and 1086 and indirectly to tyrosine 1148 of activated human epidermal growth factor receptors in intact cells. J. Biol. Chem. 269, 31310-31314 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 31310-31314
    • Okutani, T.1
  • 18
    • 33746905531 scopus 로고    scopus 로고
    • Phosphotyrosine interactome of the ErbB-receptor kinase family
    • Schulze, W. X., Deng, L. & Mann, M. Phosphotyrosine interactome of the ErbB-receptor kinase family. Mol. Syst. Biol. 1, 2005 0008 (2005).
    • (2005) Mol. Syst. Biol. , vol.1 , pp. 2005-2008
    • Schulze, W.X.1    Deng, L.2    Mann, M.3
  • 19
    • 0030854145 scopus 로고    scopus 로고
    • Positive effects of SH2 domain-containing tyrosine phosphatase SHP-1 on epidermal growth factor- and interferon-gamma-stimulated activation of STAT transcription factors in HeLa cells
    • You, M. & Zhao, Z. Positive effects of SH2 domain-containing tyrosine phosphatase SHP-1 on epidermal growth factor- and interferon-gamma-stimulated activation of STAT transcription factors in HeLa cells. J. Biol. Chem. 272, 23376-23381 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23376-23381
    • You, M.1    Zhao, Z.2
  • 20
    • 0029151931 scopus 로고
    • Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C
    • Tomic, S. et al. Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C. J. Biol. Chem. 270, 21277-21284 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21277-21284
    • Tomic, S.1
  • 21
    • 70350632734 scopus 로고    scopus 로고
    • Repression of SHP-1 expression by p53 leads to trkA tyrosine phosphorylation and suppression of breast cancer cell proliferation
    • Montano, X. Repression of SHP-1 expression by p53 leads to trkA tyrosine phosphorylation and suppression of breast cancer cell proliferation. Oncogene 28, 3787-3800 (2009).
    • (2009) Oncogene , vol.28 , pp. 3787-3800
    • Montano, X.1
  • 22
    • 0028237504 scopus 로고
    • Potent SHC tyrosine phosphorylation by epidermal growth factor at low receptor density or in the absence of receptor autophosphorylation sites
    • Soler, C., Alvarez, C. V., Beguinot, L. & Carpenter, G. Potent SHC tyrosine phosphorylation by epidermal growth factor at low receptor density or in the absence of receptor autophosphorylation sites. Oncogene 9, 2207-2215 (1994).
    • (1994) Oncogene , vol.9 , pp. 2207-2215
    • Soler, C.1    Alvarez, C.V.2    Beguinot, L.3    Carpenter, G.4
  • 23
    • 0035803494 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Grb2 by Bcr/Abl and epidermal growth factor receptor: A novel regulatory mechanism for tyrosine kinase signaling
    • Li, S., Couvillon, A. D., Brasher, B. B. & Van Etten, R. A. Tyrosine phosphorylation of Grb2 by Bcr/Abl and epidermal growth factor receptor: a novel regulatory mechanism for tyrosine kinase signaling. EMBO J. 20, 6793-6804 (2001).
    • (2001) EMBO J. , vol.20 , pp. 6793-6804
    • Li, S.1    Couvillon, A.D.2    Brasher, B.B.3    Van Etten, R.A.4
  • 24
    • 1542609420 scopus 로고    scopus 로고
    • Abl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation
    • Sini, P., Cannas, A., Koleske, A. J., Di Fiore, P. P. & Scita, G. Abl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation. Nat. Cell Biol. 6, 268-274 (2004).
    • (2004) Nat. Cell Biol. , vol.6 , pp. 268-274
    • Sini, P.1    Cannas, A.2    Koleske, A.J.3    Di Fiore, P.P.4    Scita, G.5
  • 25
    • 33845896853 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: Evolution and assessment of their pharmacological and therapeutic potential
    • Krause, C. D. et al. Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential. Pharmacol. Ther. 113, 50-87 (2007).
    • (2007) Pharmacol. Ther. , vol.113 , pp. 50-87
    • Krause, C.D.1
  • 26
    • 19744373880 scopus 로고    scopus 로고
    • A component of the nuage and pole plasm, is involved in assembly of these structures, and binds to Tudor and the methyltransferase Capsuleen
    • Anne, J. & Mechler, B. M. Valois, a component of the nuage and pole plasm, is involved in assembly of these structures, and binds to Tudor and the methyltransferase Capsuleen. Development 132, 2167-2177 (2005).
    • (2005) Development , vol.132 , pp. 2167-2177
    • Anne, J.1    Valois, M.M.B.2
  • 27
    • 78650059955 scopus 로고    scopus 로고
    • Androgen receptor coactivator p44/Mep50 in breast cancer growth and invasion
    • Peng, Y. et al. Androgen receptor coactivator p44/Mep50 in breast cancer growth and invasion. J. Cell Mol. Med. 14, 2780-2789 (2009).
    • (2009) J. Cell Mol. Med. , vol.14 , pp. 2780-2789
    • Peng, Y.1
  • 28
    • 0028957320 scopus 로고
    • In vivo and in vitro arginine methylation of RNA-binding proteins
    • Liu, Q. & Dreyfuss, G. In vivo and in vitro arginine methylation of RNA-binding proteins. Mol. Cell Biol. 15, 2800-2808 (1995).
    • (1995) Mol. Cell Biol. , vol.15 , pp. 2800-2808
    • Liu, Q.1    Dreyfuss, G.2
  • 29
    • 25444463928 scopus 로고    scopus 로고
    • PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family
    • Lee, J., Sayegh, J., Daniel, J., Clarke, S. & Bedford, M.T. PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J. Biol. Chem. 280, 32890-32896 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 32890-32896
    • Lee, J.1    Sayegh, J.2    Daniel, J.3    Clarke, S.4    Bedford, M.T.5
  • 30
    • 0031046455 scopus 로고    scopus 로고
    • The tumor suppression activity of E1A in HER-2/neu-overexpressing breast cancer
    • Chang, J. Y. et al. The tumor suppression activity of E1A in HER-2/neu-overexpressing breast cancer. Oncogene 14, 561-568 (1997).
    • (1997) Oncogene , vol.14 , pp. 561-568
    • Chang, J.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.