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Volumn 5, Issue MAY, 2014, Pages

Combining affinity proteomics and network context to identify new phosphatase substrates and adapters in growth pathways

Author keywords

Cell biology; Phosphatase; Protein protein interaction; Signal transduction; Systems biology

Indexed keywords


EID: 84905652854     PISSN: None     EISSN: 16648021     Source Type: Journal    
DOI: 10.3389/fgene.2014.00115     Document Type: Article
Times cited : (12)

References (59)
  • 1
    • 12344313069 scopus 로고    scopus 로고
    • Mutational analysis of gene families in human cancer
    • doi: 10.1016/j.gde.2004.12.009
    • Bardelli, A., and Velculescu, V. E. (2005). Mutational analysis of gene families in human cancer. Curr. Opin. Genet. Dev. 15, 5-12. doi: 10.1016/j.gde.2004.12.009
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 5-12
    • Bardelli, A.1    Velculescu, V.E.2
  • 2
    • 52649167339 scopus 로고    scopus 로고
    • Prevention of amino acid conversion in SILAC experiments with embryonic stem cells
    • doi: 10.1074/mcp.M800113-MCP200
    • Bendall, S. C., Hughes, C., Stewart, M. H., Doble, B., Bhatia, M., and Lajoie, G. A. (2008). Prevention of amino acid conversion in SILAC experiments with embryonic stem cells. Mol. Cell. Proteomics 7, 1587-1597. doi: 10.1074/mcp.M800113-MCP200
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1587-1597
    • Bendall, S.C.1    Hughes, C.2    Stewart, M.H.3    Doble, B.4    Bhatia, M.5    Lajoie, G.A.6
  • 3
    • 10644268691 scopus 로고    scopus 로고
    • Substrate-trapping techniques in the identification of cellular PTP targets
    • doi: 10.1016/j.ymeth.2004.07.007
    • Blanchetot, C., Chagnon, M., Dube, N., Halle, M., and Tremblay, M. L. (2005). Substrate-trapping techniques in the identification of cellular PTP targets. Methods 35, 44-53. doi: 10.1016/j.ymeth.2004.07.007
    • (2005) Methods , vol.35 , pp. 44-53
    • Blanchetot, C.1    Chagnon, M.2    Dube, N.3    Halle, M.4    Tremblay, M.L.5
  • 4
    • 79957915102 scopus 로고    scopus 로고
    • Disruption of intraflagellar protein transport in photoreceptor cilia causes Leber congenital amaurosis in humans and mice
    • doi: 10.1172/JCI45627
    • Boldt, K., Mans, D. A., Won, J., Van Reeuwijk, J., Vogt, A., Kinkl, N., et al. (2011). Disruption of intraflagellar protein transport in photoreceptor cilia causes Leber congenital amaurosis in humans and mice. J. Clin. Invest. 121, 2169-2180. doi: 10.1172/JCI45627
    • (2011) J. Clin. Invest. , vol.121 , pp. 2169-2180
    • Boldt, K.1    Mans, D.A.2    Won, J.3    Van Reeuwijk, J.4    Vogt, A.5    Kinkl, N.6
  • 5
    • 77953077420 scopus 로고    scopus 로고
    • A global protein kinase and phosphatase interaction network in yeast
    • doi: 10.1126/science.1176495
    • Breitkreutz, A., Choi, H., Sharom, J. R., Boucher, L., Neduva, V., Larsen, B., et al. (2010). A global protein kinase and phosphatase interaction network in yeast. Science 328, 1043-1046. doi: 10.1126/science.1176495
    • (2010) Science , vol.328 , pp. 1043-1046
    • Breitkreutz, A.1    Choi, H.2    Sharom, J.R.3    Boucher, L.4    Neduva, V.5    Larsen, B.6
  • 6
    • 67849121794 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of human embryonic stem cells
    • doi: 10.1016/j.stem.2009.06.002
    • Brill, L. M., Xiong, W., Lee, K. B., Ficarro, S. B., Crain, A., Xu, Y., et al. (2009). Phosphoproteomic analysis of human embryonic stem cells. Cell Stem Cell 5, 204-213. doi: 10.1016/j.stem.2009.06.002
    • (2009) Cell Stem Cell , vol.5 , pp. 204-213
    • Brill, L.M.1    Xiong, W.2    Lee, K.B.3    Ficarro, S.B.4    Crain, A.5    Xu, Y.6
  • 7
    • 0037078320 scopus 로고    scopus 로고
    • Gab1 and SHP-2 promote Ras/MAPK regulation of epidermal growth and differentiation
    • doi: 10.1083/jcb.200205017
    • Cai, T., Nishida, K., Hirano, T., and Khavari, P. A. (2002). Gab1 and SHP-2 promote Ras/MAPK regulation of epidermal growth and differentiation. J. Cell Biol. 159, 103-112. doi: 10.1083/jcb.200205017
    • (2002) J. Cell Biol. , vol.159 , pp. 103-112
    • Cai, T.1    Nishida, K.2    Hirano, T.3    Khavari, P.A.4
  • 8
    • 84881455143 scopus 로고    scopus 로고
    • mentha: a resource for browsing integrated protein-interaction networks
    • doi: 10.1038/nmeth.2561
    • Calderone, A., Castagnoli, L., and Cesareni, G. (2013). mentha: a resource for browsing integrated protein-interaction networks. Nat. Methods 10, 690-691. doi: 10.1038/nmeth.2561
    • (2013) Nat. Methods , vol.10 , pp. 690-691
    • Calderone, A.1    Castagnoli, L.2    Cesareni, G.3
  • 9
    • 2442717798 scopus 로고    scopus 로고
    • Mitochondrial AKAP121 binds and targets protein tyrosine phosphatase D1, a novel positive regulator of src signaling
    • doi: 10.1128/MCB.24.11.4613-4626.2004
    • Cardone, L., Carlucci, A., Affaitati, A., Livigni, A., Decristofaro, T., Garbi, C., et al. (2004). Mitochondrial AKAP121 binds and targets protein tyrosine phosphatase D1, a novel positive regulator of src signaling. Mol. Cell Biol. 24, 4613-4626. doi: 10.1128/MCB.24.11.4613-4626.2004
    • (2004) Mol. Cell Biol. , vol.24 , pp. 4613-4626
    • Cardone, L.1    Carlucci, A.2    Affaitati, A.3    Livigni, A.4    Decristofaro, T.5    Garbi, C.6
  • 10
    • 84855756033 scopus 로고    scopus 로고
    • The protein interaction network mediated by human SH3 domains
    • doi: 10.1016/j.biotechadv.2011.06.012
    • Carducci, M., Perfetto, L., Briganti, L., Paoluzi, S., Costa, S., Zerweck, J., et al. (2012). The protein interaction network mediated by human SH3 domains. Biotechnol. Adv. 30, 4-15. doi: 10.1016/j.biotechadv.2011.06.012
    • (2012) Biotechnol. Adv. , vol.30 , pp. 4-15
    • Carducci, M.1    Perfetto, L.2    Briganti, L.3    Paoluzi, S.4    Costa, S.5    Zerweck, J.6
  • 11
    • 78649837274 scopus 로고    scopus 로고
    • PTPD1 supports receptor stability and mitogenic signaling in bladder cancer cells
    • doi: 10.1074/jbc.M110.174706
    • Carlucci, A., Porpora, M., Garbi, C., Galgani, M., Santoriello, M., Mascolo, M., et al. (2010). PTPD1 supports receptor stability and mitogenic signaling in bladder cancer cells. J. Biol. Chem. 285, 39260-39270. doi: 10.1074/jbc.M110.174706
    • (2010) J. Biol. Chem. , vol.285 , pp. 39260-39270
    • Carlucci, A.1    Porpora, M.2    Garbi, C.3    Galgani, M.4    Santoriello, M.5    Mascolo, M.6
  • 12
    • 84888100485 scopus 로고    scopus 로고
    • Protein interaction network of the mammalian Hippo pathway reveals mechanisms of kinase-phosphatase interactions
    • doi: 10.1126/scisignal.2004712
    • Couzens, A. L., Knight, J. D., Kean, M. J., Teo, G., Weiss, A., Dunham, W. H., et al. (2013). Protein interaction network of the mammalian Hippo pathway reveals mechanisms of kinase-phosphatase interactions. Sci. Signal. 6, rs15. doi: 10.1126/scisignal.2004712
    • (2013) Sci. Signal. , vol.6
    • Couzens, A.L.1    Knight, J.D.2    Kean, M.J.3    Teo, G.4    Weiss, A.5    Dunham, W.H.6
  • 13
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • doi: 10.1038/nbt.1511
    • Cox, J., and Mann, M. (2008). MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372. doi: 10.1038/nbt.1511
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 14
    • 0029014973 scopus 로고
    • Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases
    • doi: 10.1126/science.7604263
    • Dent, P., Jelinek, T., Morrison, D. K., Weber, M. J., and Sturgill, T. W. (1995). Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases. Science 268, 1902-1906. doi: 10.1126/science.7604263
    • (1995) Science , vol.268 , pp. 1902-1906
    • Dent, P.1    Jelinek, T.2    Morrison, D.K.3    Weber, M.J.4    Sturgill, T.W.5
  • 15
    • 78650631004 scopus 로고    scopus 로고
    • Calcineurin increases glucose activation of ERK1/2 by reversing negative feedback
    • doi: 10.1073/pnas.1016630108
    • Duan, L., and Cobb, M. H. (2010). Calcineurin increases glucose activation of ERK1/2 by reversing negative feedback. Proc. Natl. Acad. Sci. U.S.A. 107, 22314-22319. doi: 10.1073/pnas.1016630108
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 22314-22319
    • Duan, L.1    Cobb, M.H.2
  • 16
    • 84862776164 scopus 로고    scopus 로고
    • Regulation of the phosphatase calcineurin by insulin-like growth factor I unveils a key role of astrocytes in Alzheimer's pathology
    • doi: 10.1038/mp.2011.128
    • Fernandez, A. M., Jimenez, S., Mecha, M., Davila, D., Guaza, C., Vitorica, J., et al. (2012). Regulation of the phosphatase calcineurin by insulin-like growth factor I unveils a key role of astrocytes in Alzheimer's pathology. Mol. Psychiatry 17, 705-718. doi: 10.1038/mp.2011.128
    • (2012) Mol. Psychiatry , vol.17 , pp. 705-718
    • Fernandez, A.M.1    Jimenez, S.2    Mecha, M.3    Davila, D.4    Guaza, C.5    Vitorica, J.6
  • 17
    • 0031464009 scopus 로고    scopus 로고
    • The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src
    • doi: 10.1093/emboj/16.24.7261
    • Gonfloni, S., Williams, J. C., Hattula, K., Weijland, A., Wierenga, R. K., and Superti-Furga, G. (1997). The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J. 16, 7261-7271. doi: 10.1093/emboj/16.24.7261
    • (1997) EMBO J. , vol.16 , pp. 7261-7271
    • Gonfloni, S.1    Williams, J.C.2    Hattula, K.3    Weijland, A.4    Wierenga, R.K.5    Superti-Furga, G.6
  • 18
    • 37048999786 scopus 로고    scopus 로고
    • A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes
    • doi: 10.1002/pmic.200700038
    • Gloeckner, C. J., Boldt, K., Schumacher, A., Roepman, R., and Ueffing, M. (2007). A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes. Proteomics 7, 4228-4234. doi: 10.1002/pmic.200700038
    • (2007) Proteomics , vol.7 , pp. 4228-4234
    • Gloeckner, C.J.1    Boldt, K.2    Schumacher, A.3    Roepman, R.4    Ueffing, M.5
  • 19
    • 69249083284 scopus 로고    scopus 로고
    • Strep/FLAG tandem affinity purification (SF-TAP) to study protein interactions
    • Chapter 19:Unit19.20. doi: 10.1002/0471140864.ps1920s57
    • Gloeckner, C. J., Boldt, K., and Ueffing, M. (2009). Strep/FLAG tandem affinity purification (SF-TAP) to study protein interactions. Curr. Protoc. Protein Sci. Chapter 19:Unit19.20. doi: 10.1002/0471140864.ps1920s57
    • (2009) Curr. Protoc. Protein Sci
    • Gloeckner, C.J.1    Boldt, K.2    Ueffing, M.3
  • 20
    • 59149096171 scopus 로고    scopus 로고
    • A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein
    • doi: 10.1074/mcp.M800266-MCP200
    • Goudreault, M., D'Ambrosio, L. M., Kean, M. J., Mullin, M. J., Larsen, B. G., Sanchez, A., et al. (2009). A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein. Mol. Cell. Proteomics 8, 157-171. doi: 10.1074/mcp.M800266-MCP200
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 157-171
    • Goudreault, M.1    D'Ambrosio, L.M.2    Kean, M.J.3    Mullin, M.J.4    Larsen, B.G.5    Sanchez, A.6
  • 21
    • 0032988329 scopus 로고    scopus 로고
    • Protein phosphorylation and signal transduction
    • doi: 10.1016/S0163-7258(98)00056-4
    • Graves, J. D., and Krebs, E. G. (1999). Protein phosphorylation and signal transduction. Pharmacol. Ther. 82, 111-121. doi: 10.1016/S0163-7258(98)00056-4
    • (1999) Pharmacol. Ther. , vol.82 , pp. 111-121
    • Graves, J.D.1    Krebs, E.G.2
  • 23
    • 77955285637 scopus 로고    scopus 로고
    • PP2A regulatory subunit PP2A-B' counteracts S6K phosphorylation
    • doi: 10.1016/j.cmet.2010.03.015
    • Hahn, K., Miranda, M., Francis, V. A., Vendrell, J., Zorzano, A., and Teleman, A. A. (2010). PP2A regulatory subunit PP2A-B' counteracts S6K phosphorylation. Cell Metab. 11, 438-444. doi: 10.1016/j.cmet.2010.03.015
    • (2010) Cell Metab. , vol.11 , pp. 438-444
    • Hahn, K.1    Miranda, M.2    Francis, V.A.3    Vendrell, J.4    Zorzano, A.5    Teleman, A.A.6
  • 24
    • 0034108451 scopus 로고    scopus 로고
    • Cytoskeletal protein tyrosine phosphatase PTPH1 reduces T cell antigen receptor signaling
    • doi: 10.1002/(SICI)1521-4141(200005)30:5%3C1318::AID-IMMU1318%3E3.0.CO;2-G
    • Han, S., Williams, S., and Mustelin, T. (2000). Cytoskeletal protein tyrosine phosphatase PTPH1 reduces T cell antigen receptor signaling. Eur. J. Immunol. 30, 1318-1325. doi: 10.1002/(SICI)1521-4141(200005)30:5%3C1318::AID-IMMU1318%3E3.0.CO;2-G
    • (2000) Eur. J. Immunol. , vol.30 , pp. 1318-1325
    • Han, S.1    Williams, S.2    Mustelin, T.3
  • 25
    • 84891784334 scopus 로고    scopus 로고
    • Calcineurin suppresses AMPK-dependent cytoprotective autophagy in cardiomyocytes under oxidative stress
    • doi: 10.1038/cddis.2013.533
    • He, H., Liu, X., Lv, L., Liang, H., Leng, B., Zhao, D., et al. (2014). Calcineurin suppresses AMPK-dependent cytoprotective autophagy in cardiomyocytes under oxidative stress. Cell Death Dis. 5, e997. doi: 10.1038/cddis.2013.533
    • (2014) Cell Death Dis. , vol.5
    • He, H.1    Liu, X.2    Lv, L.3    Liang, H.4    Leng, B.5    Zhao, D.6
  • 26
    • 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
    • doi: 10.1093/nar/gkr1122
    • Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B., Skrzypek, E., Murray, B., et al. (2012). PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40, D261-D270. doi: 10.1093/nar/gkr1122
    • (2012) Nucleic Acids Res. , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6
  • 27
    • 33645817920 scopus 로고    scopus 로고
    • Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26
    • doi: 10.1128/MCB.26.8.3282-3294.2006
    • Hu, Y., and Mivechi, N. F. (2006). Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26. Mol. Cell. Biol. 26, 3282-3294. doi: 10.1128/MCB.26.8.3282-3294.2006
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3282-3294
    • Hu, Y.1    Mivechi, N.F.2
  • 28
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • doi: 10.1038/nprot.2008.211
    • Huang da, W., Sherman, B. T., and Lempicki, R. A. (2009). Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44-57. doi: 10.1038/nprot.2008.211
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 29
    • 77956283656 scopus 로고    scopus 로고
    • A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability
    • doi: 10.1101/gad.1934210
    • Hurov, K. E., Cotta-Ramusino, C., and Elledge, S. J. (2010). A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability. Genes Dev. 24, 1939-1950. doi: 10.1101/gad.1934210
    • (2010) Genes Dev. , vol.24 , pp. 1939-1950
    • Hurov, K.E.1    Cotta-Ramusino, C.2    Elledge, S.J.3
  • 30
    • 78650601353 scopus 로고    scopus 로고
    • Inside the human cancer tyrosine phosphatome
    • doi: 10.1038/nrc2980
    • Julien, S. G., Dube, N., Hardy, S., and Tremblay, M. L. (2011). Inside the human cancer tyrosine phosphatome. Nat. Rev. Cancer 11, 35-49. doi: 10.1038/nrc2980
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 35-49
    • Julien, S.G.1    Dube, N.2    Hardy, S.3    Tremblay, M.L.4
  • 31
    • 59149101536 scopus 로고    scopus 로고
    • Calcineurin/NFAT signaling is required for neuregulin-regulated Schwann cell differentiation
    • doi: 10.1126/science.1166562
    • Kao, S. C., Wu, H., Xie, J., Chang, C. P., Ranish, J. A., Graef, I. A., et al. (2009). Calcineurin/NFAT signaling is required for neuregulin-regulated Schwann cell differentiation. Science 323, 651-654. doi: 10.1126/science.1166562
    • (2009) Science , vol.323 , pp. 651-654
    • Kao, S.C.1    Wu, H.2    Xie, J.3    Chang, C.P.4    Ranish, J.A.5    Graef, I.A.6
  • 32
    • 84894597311 scopus 로고    scopus 로고
    • The DUSP26 phosphatase activator adenylate kinase 2 regulates FADD phosphorylation and cell growth
    • doi: 10.1038/ncomms4351
    • Kim, H., Lee, H. J., Oh, Y., Choi, S. G., Hong, S. H., Kim, H. J., et al. (2014). The DUSP26 phosphatase activator adenylate kinase 2 regulates FADD phosphorylation and cell growth. Nat. Commun. 5, 3351. doi: 10.1038/ncomms4351
    • (2014) Nat. Commun. , vol.5 , pp. 3351
    • Kim, H.1    Lee, H.J.2    Oh, Y.3    Choi, S.G.4    Hong, S.H.5    Kim, H.J.6
  • 33
    • 84877992759 scopus 로고    scopus 로고
    • Elucidating human phosphatase-substrate networks
    • doi: 10.1126/scisignal.2003203
    • Li, X., Wilmanns, M., Thornton, J., and Kohn, M. (2013). Elucidating human phosphatase-substrate networks. Sci. Signal. 6, rs10. doi: 10.1126/scisignal.2003203
    • (2013) Sci. Signal. , vol.6
    • Li, X.1    Wilmanns, M.2    Thornton, J.3    Kohn, M.4
  • 34
    • 84884322287 scopus 로고    scopus 로고
    • ATM pathway is essential for ionizing radiation-induced autophagy
    • doi: 10.1016/j.cellsig.2013.08.010
    • Liang, N., Jia, L., Liu, Y., Liang, B., Kong, D., Yan, M., et al. (2013). ATM pathway is essential for ionizing radiation-induced autophagy. Cell. Signal. 25, 2530-2539. doi: 10.1016/j.cellsig.2013.08.010
    • (2013) Cell. Signal. , vol.25 , pp. 2530-2539
    • Liang, N.1    Jia, L.2    Liu, Y.3    Liang, B.4    Kong, D.5    Yan, M.6
  • 35
    • 84872816249 scopus 로고    scopus 로고
    • HuPho: the human phosphatase portal
    • doi: 10.1111/j.1742-4658.2012.08712.x
    • Liberti, S., Sacco, F., Calderone, A., Perfetto, L., Iannuccelli, M., Panni, S., et al. (2013). HuPho: the human phosphatase portal. FEBS J. 280, 379-387. doi: 10.1111/j.1742-4658.2012.08712.x
    • (2013) FEBS J. , vol.280 , pp. 379-387
    • Liberti, S.1    Sacco, F.2    Calderone, A.3    Perfetto, L.4    Iannuccelli, M.5    Panni, S.6
  • 36
    • 84870512554 scopus 로고    scopus 로고
    • PP2A blockade inhibits autophagy and causes intraneuronal accumulation of ubiquitinated proteins
    • doi: 10.1016/j.neurobiolaging.2012.06.026
    • Magnaudeix, A., Wilson, C. M., Page, G., Bauvy, C., Codogno, P., Leveque, P., et al. (2013). PP2A blockade inhibits autophagy and causes intraneuronal accumulation of ubiquitinated proteins. Neurobiol. Aging 34, 770-790. doi: 10.1016/j.neurobiolaging.2012.06.026
    • (2013) Neurobiol. Aging , vol.34 , pp. 770-790
    • Magnaudeix, A.1    Wilson, C.M.2    Page, G.3    Bauvy, C.4    Codogno, P.5    Leveque, P.6
  • 37
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • doi: 10.1038/nbt0303-255
    • Mann, M., and Jensen, O. N. (2003). Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21, 255-261. doi: 10.1038/nbt0303-255
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 38
    • 0036806311 scopus 로고    scopus 로고
    • Evolution of protein kinase signaling from yeast to man
    • doi: 10.1016/S0968-0004(02)02179-5
    • Manning, G., Plowman, G. D., Hunter, T., and Sudarsanam, S. (2002a). Evolution of protein kinase signaling from yeast to man. Trends Biochem. Sci. 27, 514-520. doi: 10.1016/S0968-0004(02)02179-5
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 514-520
    • Manning, G.1    Plowman, G.D.2    Hunter, T.3    Sudarsanam, S.4
  • 39
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • doi: 10.1126/science.1075762
    • Manning, G., Whyte, D. B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002b). The protein kinase complement of the human genome. Science 298, 1912-1934. doi: 10.1126/science.1075762
    • (2002) Science , vol.298 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 40
    • 78651065696 scopus 로고    scopus 로고
    • A QUICK screen for Lrrk2 interaction partners-leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics
    • doi: 10.1074/mcp.M110.001172
    • Meixner, A., Boldt, K., Van Troys, M., Askenazi, M., Gloeckner, C. J., Bauer, M., et al. (2011). A QUICK screen for Lrrk2 interaction partners-leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics. Mol. Cell. Proteomics 10, M110 001172. doi: 10.1074/mcp.M110.001172
    • (2011) Mol. Cell. Proteomics , vol.10
    • Meixner, A.1    Boldt, K.2    Van Troys, M.3    Askenazi, M.4    Gloeckner, C.J.5    Bauer, M.6
  • 41
    • 77957154303 scopus 로고    scopus 로고
    • The cell polarity regulator hScrib controls ERK activation through a KIM site-dependent interaction
    • doi: 10.1038/onc.2010.265
    • Nagasaka, K., Pim, D., Massimi, P., Thomas, M., Tomaic, V., Subbaiah, V. K., et al. (2010). The cell polarity regulator hScrib controls ERK activation through a KIM site-dependent interaction. Oncogene 29, 5311-5321. doi: 10.1038/onc.2010.265
    • (2010) Oncogene , vol.29 , pp. 5311-5321
    • Nagasaka, K.1    Pim, D.2    Massimi, P.3    Thomas, M.4    Tomaic, V.5    Subbaiah, V.K.6
  • 42
    • 84872862228 scopus 로고    scopus 로고
    • A novel interaction between hScrib and PP1gamma downregulates ERK signaling and suppresses oncogene-induced cell transformation
    • doi: 10.1371/journal.pone.0053752
    • Nagasaka, K., Seiki, T., Yamashita, A., Massimi, P., Subbaiah, V. K., Thomas, M., et al. (2013). A novel interaction between hScrib and PP1gamma downregulates ERK signaling and suppresses oncogene-induced cell transformation. PLoS ONE 8:e53752. doi: 10.1371/journal.pone.0053752
    • (2013) PLoS ONE , vol.8
    • Nagasaka, K.1    Seiki, T.2    Yamashita, A.3    Massimi, P.4    Subbaiah, V.K.5    Thomas, M.6
  • 43
    • 29244448703 scopus 로고    scopus 로고
    • Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap
    • doi: 10.1074/mcp.T500030-MCP200
    • Olsen, J. V., de Godoy, L. M., Li, G., Macek, B., Mortensen, P., Pesch, R., et al. (2005). Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap. Mol. Cell. Proteomics 4, 2010-2021. doi: 10.1074/mcp.T500030-MCP200
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 2010-2021
    • Olsen, J.V.1    de Godoy, L.M.2    Li, G.3    Macek, B.4    Mortensen, P.5    Pesch, R.6
  • 44
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • doi: 10.1074/mcp.M200025-MCP200
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., et al. (2002). Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386. doi: 10.1074/mcp.M200025-MCP200
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 45
    • 77954951974 scopus 로고    scopus 로고
    • DUSP26 negatively affects the proliferation of epithelial cells, an effect not mediated by dephosphorylation of MAPKs
    • doi: 10.1016/j.bbamcr.2010.03.014
    • Patterson, K. I., Brummer, T., Daly, R. J., and O'Brien, P. M. (2010). DUSP26 negatively affects the proliferation of epithelial cells, an effect not mediated by dephosphorylation of MAPKs. Biochim. Biophys. Acta 1803, 1003-1012. doi: 10.1016/j.bbamcr.2010.03.014
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 1003-1012
    • Patterson, K.I.1    Brummer, T.2    Daly, R.J.3    O'Brien, P.M.4
  • 46
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • doi: 10.1016/j.cell.2007.11.025
    • Rikova, K., Guo, A., Zeng, Q., Possemato, A., Yu, J., Haack, H., et al. (2007). Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 131, 1190-1203. doi: 10.1016/j.cell.2007.11.025
    • (2007) Cell , vol.131 , pp. 1190-1203
    • Rikova, K.1    Guo, A.2    Zeng, Q.3    Possemato, A.4    Yu, J.5    Haack, H.6
  • 47
    • 77449110096 scopus 로고    scopus 로고
    • Cracking the phosphatase code: docking interactions determine substrate specificity
    • doi: 10.1126/scisignal.2100re9
    • Roy, J., and Cyert, M. S. (2009). Cracking the phosphatase code: docking interactions determine substrate specificity. Sci. Signal. 2, re9. doi: 10.1126/scisignal.2100re9
    • (2009) Sci. Signal. , vol.2
    • Roy, J.1    Cyert, M.S.2
  • 49
    • 84864583212 scopus 로고    scopus 로고
    • The human phosphatase interactome: an intricate family portrait
    • doi: 10.1016/j.febslet.2012.05.008
    • Sacco, F., Perfetto, L., Castagnoli, L., and Cesareni, G. (2012b). The human phosphatase interactome: an intricate family portrait. FEBS Lett. 586, 2732-2739. doi: 10.1016/j.febslet.2012.05.008
    • (2012) FEBS Lett. , vol.586 , pp. 2732-2739
    • Sacco, F.1    Perfetto, L.2    Castagnoli, L.3    Cesareni, G.4
  • 50
    • 77956341371 scopus 로고    scopus 로고
    • Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma
    • doi: 10.1038/onc.2010.244
    • Shang, X., Vasudevan, S. A., Yu, Y., Ge, N., Ludwig, A. D., Wesson, C. L., et al. (2010). Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma. Oncogene 29, 4938-4946. doi: 10.1038/onc.2010.244
    • (2010) Oncogene , vol.29 , pp. 4938-4946
    • Shang, X.1    Vasudevan, S.A.2    Yu, Y.3    Ge, N.4    Ludwig, A.D.5    Wesson, C.L.6
  • 51
    • 79953713220 scopus 로고    scopus 로고
    • Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5
    • doi: 10.1002/pmic.201000770
    • Skarra, D. V., Goudreault, M., Choi, H., Mullin, M., Nesvizhskii, A. I., Gingras, A. C., et al. (2011). Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5. Proteomics 11, 1508-1516. doi: 10.1002/pmic.201000770
    • (2011) Proteomics , vol.11 , pp. 1508-1516
    • Skarra, D.V.1    Goudreault, M.2    Choi, H.3    Mullin, M.4    Nesvizhskii, A.I.5    Gingras, A.C.6
  • 52
    • 0037123768 scopus 로고    scopus 로고
    • Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways
    • doi: 10.1016/S0092-8674(02)00747-X
    • Taniguchi, T., Garcia-Higuera, I., Xu, B., Andreassen, P. R., Gregory, R. C., Kim, S. T., et al. (2002). Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways. Cell 109, 459-472. doi: 10.1016/S0092-8674(02)00747-X
    • (2002) Cell , vol.109 , pp. 459-472
    • Taniguchi, T.1    Garcia-Higuera, I.2    Xu, B.3    Andreassen, P.R.4    Gregory, R.C.5    Kim, S.T.6
  • 53
    • 59649115613 scopus 로고    scopus 로고
    • Protein phosphatase Dusp26 associates with KIF3 motor and promotes N-cadherin-mediated cell-cell adhesion
    • doi: 10.1038/onc.2008.431
    • Tanuma, N., Nomura, M., Ikeda, M., Kasugai, I., Tsubaki, Y., Takagaki, K., et al. (2009). Protein phosphatase Dusp26 associates with KIF3 motor and promotes N-cadherin-mediated cell-cell adhesion. Oncogene 28, 752-761. doi: 10.1038/onc.2008.431
    • (2009) Oncogene , vol.28 , pp. 752-761
    • Tanuma, N.1    Nomura, M.2    Ikeda, M.3    Kasugai, I.4    Tsubaki, Y.5    Takagaki, K.6
  • 54
    • 54749086397 scopus 로고    scopus 로고
    • A specificity map for the PDZ domain family
    • doi: 10.1371/journal.pbio.0060239
    • Tonikian, R., Zhang, Y., Sazinsky, S. L., Currell, B., Yeh, J. H., Reva, B., et al. (2008). A specificity map for the PDZ domain family. PLoS Biol. 6:e239. doi: 10.1371/journal.pbio.0060239
    • (2008) PLoS Biol. , vol.6
    • Tonikian, R.1    Zhang, Y.2    Sazinsky, S.L.3    Currell, B.4    Yeh, J.H.5    Reva, B.6
  • 55
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: from genes, to function, to disease
    • doi: 10.1038/nrm2039
    • Tonks, N. K. (2006). Protein tyrosine phosphatases: from genes, to function, to disease. Nat. Rev. Mol. Cell Biol. 7, 833-846. doi: 10.1038/nrm2039
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 56
    • 58249087616 scopus 로고    scopus 로고
    • The PTP family photo album
    • doi: 10.1016/j.cell.2009.01.006
    • Tremblay, M. L. (2009). The PTP family photo album. Cell 136, 213-214. doi: 10.1016/j.cell.2009.01.006
    • (2009) Cell , vol.136 , pp. 213-214
    • Tremblay, M.L.1
  • 57
    • 84881413580 scopus 로고    scopus 로고
    • Reactive nitrogen species regulate autophagy through ATM-AMPK-TSC2-mediated suppression of mTORC1
    • doi: 10.1073/pnas.1307736110
    • Tripathi, D. N., Chowdhury, R., Trudel, L. J., Tee, A. R., Slack, R. S., Walker, C. L., et al. (2013). Reactive nitrogen species regulate autophagy through ATM-AMPK-TSC2-mediated suppression of mTORC1. Proc. Natl. Acad. Sci. U.S.A. 110, E2950-E2957. doi: 10.1073/pnas.1307736110
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110
    • Tripathi, D.N.1    Chowdhury, R.2    Trudel, L.J.3    Tee, A.R.4    Slack, R.S.5    Walker, C.L.6
  • 58
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera, S., and Hemmings, B. A. (1995). Serine/threonine protein phosphatases. Biochem. J. 311(pt 1), 17-29.
    • (1995) Biochem. J. , vol.311 , Issue.PART 1 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 59
    • 8844253220 scopus 로고    scopus 로고
    • SHP2 binds catalase and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling
    • doi: 10.1016/j.febslet.2004.10.011
    • Yano, S., Arroyo, N., and Yano, N. (2004). SHP2 binds catalase and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling. FEBS Lett. 577, 327-332. doi: 10.1016/j.febslet.2004.10.011
    • (2004) FEBS Lett. , vol.577 , pp. 327-332
    • Yano, S.1    Arroyo, N.2    Yano, N.3


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