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Volumn 8, Issue 5, 2012, Pages 1452-1460

Probing protein phosphatase substrate binding: Affinity pull-down of ILKAP phosphatase 2C with phosphopeptides

Author keywords

[No Author keywords available]

Indexed keywords

ANAZOLENE SODIUM; ATM PROTEIN; CELL CYCLE PROTEIN; CHECKPOINT KINASE 1; CHECKPOINT KINASE 2; DNA BINDING PROTEIN; FUCHSINE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHOPEPTIDE; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2C; PROTEIN KINASE; PROTEIN P53; PROTEIN SERINE THREONINE KINASE; RIBOSOMAL PROTEIN S6 KINASE, 90KDA, POLYPEPTIDE 3; S6 KINASE; TUMOR SUPPRESSOR PROTEIN;

EID: 84859856421     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/c2mb05478g     Document Type: Article
Times cited : (6)

References (42)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling - 2000 and beyond
    • T. Hunter Signaling - 2000 and Beyond Cell (Cambridge, Mass.) 2000 100 113 127
    • (2000) Cell (Cambridge, Mass.) , vol.100 , pp. 113-127
    • Hunter, T.1
  • 4
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • D. Barford A. K. Das M. P. Egloff The structure and mechanism of protein phosphatases: Insights into catalysis and regulation Annu. Rev. Biophys. Biomol. Struct. 1998 27 133 164
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 5
    • 70350340056 scopus 로고    scopus 로고
    • Serine/Threonine Phosphatases: Mechanism through Structure
    • Y. Shi Serine/Threonine Phosphatases: Mechanism through Structure Cell (Cambridge, Mass.) 2009 139 468 484
    • (2009) Cell (Cambridge, Mass.) , vol.139 , pp. 468-484
    • Shi, Y.1
  • 6
    • 36849053513 scopus 로고    scopus 로고
    • Role of Type 2C Protein Phosphatases in Growth Regulation and in Cellular Stress Signaling
    • T. Lammers S. Lavi Role of Type 2C Protein Phosphatases in Growth Regulation and in Cellular Stress Signaling Crit. Rev. Biochem. Mol. Biol. 2007 42 437 461
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 437-461
    • Lammers, T.1    Lavi, S.2
  • 7
    • 33845881426 scopus 로고    scopus 로고
    • Evolution of the Metazoan Protein Phosphatase 2C Superfamily
    • A. Stern E. Privman M. Rasis S. Lavi T. Pupko Evolution of the Metazoan Protein Phosphatase 2C Superfamily J. Mol. Evol. 2007 64 61 70
    • (2007) J. Mol. Evol. , vol.64 , pp. 61-70
    • Stern, A.1    Privman, E.2    Rasis, M.3    Lavi, S.4    Pupko, T.5
  • 8
    • 0035341207 scopus 로고    scopus 로고
    • Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1
    • C. Leung-Hagesteijn A. Mahendra I. Naruszewicz G. E. Hannigan Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1 EMBO J. 2001 20 2160 2170
    • (2001) EMBO J. , vol.20 , pp. 2160-2170
    • Leung-Hagesteijn, C.1    Mahendra, A.2    Naruszewicz, I.3    Hannigan, G.E.4
  • 12
    • 33748595526 scopus 로고    scopus 로고
    • Mechanism-Based Profiling of Enzyme Families
    • M. J. Evans B. F. Cravatt Mechanism-Based Profiling of Enzyme Families Chem. Rev. 2006 106 3279 3301
    • (2006) Chem. Rev. , vol.106 , pp. 3279-3301
    • Evans, M.J.1    Cravatt, B.F.2
  • 14
    • 77957707285 scopus 로고    scopus 로고
    • Serine/Threonine Protein Phosphatase Assays
    • T. McAvoy A. C. Nairn Serine/Threonine Protein Phosphatase Assays Curr. Protocol Mol. Biol. 2010 92 18.18.11 18.18.11
    • (2010) Curr. Protocol Mol. Biol. , vol.92 , pp. 181811-181811
    • McAvoy, T.1    Nairn, A.C.2
  • 15
    • 14044251529 scopus 로고    scopus 로고
    • Specific Inactivation and Nuclear Anchoring of Extracellular Signal-Regulated Kinase 2 by the Inducible Dual-Specificity Protein Phosphatase DUSP5
    • M. Mandl D. N. Slack S. M. Keyse Specific Inactivation and Nuclear Anchoring of Extracellular Signal-Regulated Kinase 2 by the Inducible Dual-Specificity Protein Phosphatase DUSP5 Mol. Cell Biol. 2005 25 1830 1845
    • (2005) Mol. Cell Biol. , vol.25 , pp. 1830-1845
    • Mandl, M.1    Slack, D.N.2    Keyse, S.M.3
  • 16
    • 34247572838 scopus 로고    scopus 로고
    • Proteomic approaches to studying protein tyrosine phosphatases
    • F. Liang S. Kumar Z.-Y. Zhang Proteomic approaches to studying protein tyrosine phosphatases Mol. Biosyst. 2007 3 308 316
    • (2007) Mol. Biosyst. , vol.3 , pp. 308-316
    • Liang, F.1    Kumar, S.2    Zhang, Z.-Y.3
  • 19
    • 70349128914 scopus 로고    scopus 로고
    • Profiling protein tyrosine phosphatase activity with mechanistic probes
    • D. Krishnamurthy A. M. Barrios Profiling protein tyrosine phosphatase activity with mechanistic probes Curr. Opin. Chem. Biol. 2009 13 375 381
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 375-381
    • Krishnamurthy, D.1    Barrios, A.M.2
  • 23
    • 4344560876 scopus 로고    scopus 로고
    • The p53-Induced Oncogenic Phosphatase PPM1D Interacts with Uracil DNA Glycosylase and Suppresses Base Excision Repair
    • X. Lu D. Bocangel B. Nannenga H. Yamaguchi E. Appella L. A. Donehower The p53-Induced Oncogenic Phosphatase PPM1D Interacts with Uracil DNA Glycosylase and Suppresses Base Excision Repair Mol. Cell 2004 15 621 634
    • (2004) Mol. Cell , vol.15 , pp. 621-634
    • Lu, X.1    Bocangel, D.2    Nannenga, B.3    Yamaguchi, H.4    Appella, E.5    Donehower, L.A.6
  • 24
    • 18844405191 scopus 로고    scopus 로고
    • PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle checkpoints
    • X. B. Lu B. Nannenga L. A. Donehower PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle checkpoints Genes Dev. 2005 19 1162 1174
    • (2005) Genes Dev. , vol.19 , pp. 1162-1174
    • Lu, X.B.1    Nannenga, B.2    Donehower, L.A.3
  • 27
    • 4544241565 scopus 로고    scopus 로고
    • P90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2C delta
    • U. Doehn S. Gammeltoft S. H. Shen C. J. Jensen p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2C delta Biochem. J. 2004 382 425 431
    • (2004) Biochem. J. , vol.382 , pp. 425-431
    • Doehn, U.1    Gammeltoft, S.2    Shen, S.H.3    Jensen, C.J.4
  • 28
    • 0026704473 scopus 로고
    • PEGA - A Flow Stable Polyethylene-Glycol Dimethyl Acrylamide Copolymer for Solid-Phase Synthesis
    • M. Meldal PEGA - A Flow Stable Polyethylene-Glycol Dimethyl Acrylamide Copolymer for Solid-Phase Synthesis Tetrahedron Lett. 1992 33 3077
    • (1992) Tetrahedron Lett. , vol.33 , pp. 3077
    • Meldal, M.1
  • 29
    • 0032147436 scopus 로고    scopus 로고
    • Synthesis and characterization of polyethylene glycol polyacrylamide copolymer (PEGA) resins containing carbohydrate ligands. Evaluation as supports for affinity chromatography
    • F. I. Auzanneau M. K. Christensen S. L. Harris M. Meldal B. M. Pinto Synthesis and characterization of polyethylene glycol polyacrylamide copolymer (PEGA) resins containing carbohydrate ligands. Evaluation as supports for affinity chromatography Can. J. Chem. 1998 76 1109
    • (1998) Can. J. Chem. , vol.76 , pp. 1109
    • Auzanneau, F.I.1    Christensen, M.K.2    Harris, S.L.3    Meldal, M.4    Pinto, B.M.5
  • 30
    • 33751185559 scopus 로고    scopus 로고
    • Microwave heating for solid-phase peptide synthesis: General evaluation and application to 15 mer phosphopeptides
    • M. Brandt S. Gammeltoft K. J. Jensen Microwave heating for solid-phase peptide synthesis: General evaluation and application to 15 mer phosphopeptides Int. J. Pept. Res. Ther. 2006 12 349 357
    • (2006) Int. J. Pept. Res. Ther. , vol.12 , pp. 349-357
    • Brandt, M.1    Gammeltoft, S.2    Jensen, K.J.3
  • 33
    • 0020395778 scopus 로고
    • Synthesis of the Antibacterial Peptide Cecropin A(1-33)
    • R. B. Merrifield L. D. Vizioli H. G. Boman Synthesis of the Antibacterial Peptide Cecropin A(1-33) Biochemistry 1982 21 5020 5031
    • (1982) Biochemistry , vol.21 , pp. 5020-5031
    • Merrifield, R.B.1    Vizioli, L.D.2    Boman, H.G.3
  • 34
    • 48449104617 scopus 로고    scopus 로고
    • GOEAST: A web-based software toolkit for Gene Ontology enrichment analysis
    • Q. Zheng X.-J. Wang GOEAST: a web-based software toolkit for Gene Ontology enrichment analysis Nucleic Acids Res. 2008 36 W358 W363
    • (2008) Nucleic Acids Res. , vol.36
    • Zheng, Q.1    Wang, X.-J.2
  • 35
    • 0038418869 scopus 로고    scopus 로고
    • Chk1 and Chk2 kinases in checkpoint control and cancer
    • J. Bartek J. Lukas Chk1 and Chk2 kinases in checkpoint control and cancer Cancer Cell 2003 3 421 429
    • (2003) Cancer Cell , vol.3 , pp. 421-429
    • Bartek, J.1    Lukas, J.2
  • 36
    • 43049128122 scopus 로고    scopus 로고
    • The type 2C phosphatase Wip1: An oncogenic regulator of tumor suppressor and DNA damage response pathways
    • X. Lu T.-A. Nguyen S.-H. Moon Y. Darlington M. Sommer L. A. Donehower The type 2C phosphatase Wip1: An oncogenic regulator of tumor suppressor and DNA damage response pathways Cancer Metastasis Rev. 2008 27 123 135
    • (2008) Cancer Metastasis Rev. , vol.27 , pp. 123-135
    • Lu, X.1    Nguyen, T.-A.2    Moon, S.-H.3    Darlington, Y.4    Sommer, M.5    Donehower, L.A.6
  • 38
    • 0040175067 scopus 로고    scopus 로고
    • Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction
    • M. Frödin S. Gammeltoft Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction Mol. Cell. Endocrinol. 1999 151 65 77
    • (1999) Mol. Cell. Endocrinol. , vol.151 , pp. 65-77
    • Frödin, M.1    Gammeltoft, S.2
  • 39
    • 33748320817 scopus 로고    scopus 로고
    • RSK and MSK in MAP kinase signalling
    • C. Hauge M. Frödin RSK and MSK in MAP kinase signalling J. Cell Sci. 2006 119 3021 3023
    • (2006) J. Cell Sci. , vol.119 , pp. 3021-3023
    • Hauge, C.1    Frödin, M.2
  • 40
    • 0242612949 scopus 로고    scopus 로고
    • A Phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1
    • M. Frodin C. J. Jensen K. Merienne S. Gammeltoft A Phosphoserine- regulated docking site in the protein kinase RSK2 that recruits and activates PDK1 EMBO J. 2000 19 2924 2934
    • (2000) EMBO J. , vol.19 , pp. 2924-2934
    • Frodin, M.1    Jensen, C.J.2    Merienne, K.3    Gammeltoft, S.4
  • 41
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • A. Shevchenko H. Tomas J. Havlis J. V. Olsen M. Mann In-gel digestion for mass spectrometric characterization of proteins and proteomes Nat. Protocols 2006 1 2856 2860
    • (2006) Nat. Protocols , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 42
    • 53049101603 scopus 로고    scopus 로고
    • TiO2-Based Phosphoproteomic Analysis of the Plasma Membrane and the Effects of Phosphatase Inhibitor Treatment
    • T. E. Thingholm M. R. Larsen C. R. Ingrell M. Kassem O. N. Jensen TiO2-Based Phosphoproteomic Analysis of the Plasma Membrane and the Effects of Phosphatase Inhibitor Treatment J. Proteome Res. 2008 7 3304 3313
    • (2008) J. Proteome Res. , vol.7 , pp. 3304-3313
    • Thingholm, T.E.1    Larsen, M.R.2    Ingrell, C.R.3    Kassem, M.4    Jensen, O.N.5


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