메뉴 건너뛰기




Volumn 418, Issue 2, 2011, Pages 267-275

A general strategy for studying multisite protein phosphorylation using label-free selected reaction monitoring mass spectrometry

Author keywords

Enzymatic assay; Kinase; Label free quantification; Mass spectrometry; Phosphatase; Phosphorylation; Selected reaction monitoring

Indexed keywords

MASS SPECTROMETRY; PHOSPHATASES; SUBSTRATES;

EID: 81155161026     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.07.015     Document Type: Article
Times cited : (13)

References (42)
  • 2
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • J.V. Olsen, B. Blagoev, F. Gnad, B. Macek, C. Kumar, P. Mortensen, and M. Mann Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 127 2006 635 648 (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 3
    • 0346363801 scopus 로고    scopus 로고
    • Mitotic regulation of the human anaphase-promoting complex by phosphorylation
    • DOI 10.1093/emboj/cdg627
    • C. Kraft, F. Herzog, C. Gieffers, K. Mechtler, A. Hagting, J. Pines, and J.M. Peters Mitotic regulation of the human anaphase-promoting complex by phosphorylation EMBO J. 22 2003 6598 6609 (Pubitemid 38009606)
    • (2003) EMBO Journal , vol.22 , Issue.24 , pp. 6598-6609
    • Kraft, C.1    Herzog, F.2    Gieffers, C.3    Mechtler, K.4    Hagting, A.5    Pines, J.6    Peters, J.-M.7
  • 5
    • 0031991880 scopus 로고    scopus 로고
    • PKA and MPF-activated polo-like kinase regulate anaphase-promoting complex activity and mitosis progression
    • S. Kotani, S. Tugendreich, M. Fujii, P.M. Jorgensen, N. Watanabe, C. Hoog, P. Hieter, and K. Todokoro PKA and MPF-activated polo-like kinase regulate anaphase-promoting complex activity and mitosis progression Mol. Cell 1 1998 371 380 (Pubitemid 128378885)
    • (1998) Molecular Cell , vol.1 , Issue.3 , pp. 371-380
    • Kotani, S.1    Tugendreich, S.2    Fujii, M.3    Jorgensen, P.-M.4    Watanabe, N.5    Hoog, C.6    Hieter, P.7    Todokoro, K.8
  • 6
    • 0033598127 scopus 로고    scopus 로고
    • Regulation of APC activity by phosphorylation and regulatory factors
    • DOI 10.1083/jcb.146.4.791
    • S. Kotani, H. Tanaka, H. Yasuda, and K. Todokoro Regulation of APC activity by phosphorylation and regulatory factors J. Cell Biol. 146 1999 791 800 (Pubitemid 29408905)
    • (1999) Journal of Cell Biology , vol.146 , Issue.4 , pp. 791-800
    • Kotani, S.1    Tanaka, H.2    Yasuda, H.3    Todokoro, K.4
  • 7
    • 0034717570 scopus 로고    scopus 로고
    • Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the anaphase-promoting complex
    • DOI 10.1083/jcb.149.7.1377
    • A.D. Rudner, and A.W. Murray Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the anaphase-promoting complex J. Cell Biol. 149 2000 1377 1390 (Pubitemid 30437613)
    • (2000) Journal of Cell Biology , vol.149 , Issue.7 , pp. 1377-1390
    • Rudner, A.D.1    Murray, A.W.2
  • 8
    • 0037013326 scopus 로고    scopus 로고
    • The cyclin-ubiquitin ligase activity of cyclosome/APC is jointly activated by protein kinases Cdk1-cyclin B and Plk
    • DOI 10.1074/jbc.M111476200
    • A. Golan, Y. Yudkovsky, and A. Hershko The cyclin-ubiquitin ligase activity of cyclosome/APC is jointly activated by protein kinases Cdk1-cyclin B and Plk J. Biol. Chem. 277 2002 15552 15557 (Pubitemid 34967823)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15552-15557
    • Golan, A.1    Yudkovsky, Y.2    Hershko, A.3
  • 9
    • 7744230752 scopus 로고    scopus 로고
    • Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C inhibition by the spindle checkpoint
    • DOI 10.1016/j.molcel.2004.09.031, PII S1097276504005830
    • Z. Tang, H. Shu, D. Oncel, S. Chen, and H. Yu Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C inhibition by the spindle checkpoint Mol. Cell 16 2004 387 397 (Pubitemid 39504793)
    • (2004) Molecular Cell , vol.16 , Issue.3 , pp. 387-397
    • Tang, Z.1    Shu, H.2    Oncel, D.3    Chen, S.4    Yu, H.5
  • 11
    • 0032573374 scopus 로고    scopus 로고
    • Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex
    • W. Zachariae, M. Schwab, K. Nasmyth, and W. Seufert Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex Science 282 1998 1721 1724 (Pubitemid 28549290)
    • (1998) Science , vol.282 , Issue.5394 , pp. 1721-1724
    • Zachariae, W.1    Schwab, M.2    Nasmyth, K.3    Seufert, W.4
  • 12
    • 1642602693 scopus 로고    scopus 로고
    • The DNA damage checkpoint and PKA pathways converge on APC substrates and Cdc20 to regulate mitotic progression
    • DOI 10.1038/ncb1092
    • J.S. Searle, K.L. Schollaert, B.J. Wilkins, and Y. Sanchez The DNA damage checkpoint and PKA pathways converge on APC substrates and Cdc20 to regulate mitotic progression Nat. Cell Biol. 6 2004 138 145 (Pubitemid 38425713)
    • (2004) Nature Cell Biology , vol.6 , Issue.2 , pp. 138-145
    • Searle, J.S.1    Schollaert, K.L.2    Wilkins, B.J.3    Sanchez, Y.4
  • 13
  • 14
    • 74049115774 scopus 로고    scopus 로고
    • Mass spectrometry-based label-free quantitative proteomics
    • W. Zhu, J.W. Smith, and C.M. Huang Mass spectrometry-based label-free quantitative proteomics J. Biomed. Biotechnol. 2010 840518
    • (2010) J. Biomed. Biotechnol. , pp. 840518
    • Zhu, W.1    Smith, J.W.2    Huang, C.M.3
  • 17
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • S.E. Ong, and M. Mann Mass spectrometry-based proteomics turns quantitative Nat. Chem. Biol. 1 2005 252 262
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 20
    • 33745621292 scopus 로고    scopus 로고
    • Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry
    • DOI 10.1074/mcp.T500029-MCP200
    • V. Mayya, K. Rezual, L. Wu, M.B. Fong, and D.K. Han Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry: determination of inhibitory phosphorylation status of cyclin-dependent kinases Mol. Cell. Proteomics 5 2006 1146 1157 (Pubitemid 43985937)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.6 , pp. 1146-1157
    • Mayya, V.1    Rezual, K.2    Wu, L.3    Fong, M.B.4    Han, D.K.5
  • 22
    • 67650886056 scopus 로고    scopus 로고
    • A site-specific, multiplexed kinase activity assay using stable-isotope dilution and high-resolution mass spectrometry
    • Y. Yu, R. Anjum, K. Kubota, J. Rush, J. Villen, and S.P. Gygi A site-specific, multiplexed kinase activity assay using stable-isotope dilution and high-resolution mass spectrometry Proc. Natl. Acad. Sci. USA 106 2009 11606 11611
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 11606-11611
    • Yu, Y.1    Anjum, R.2    Kubota, K.3    Rush, J.4    Villen, J.5    Gygi, S.P.6
  • 23
    • 77954185457 scopus 로고    scopus 로고
    • Assay development for the determination of phosphorylation stoichiometry using multiple reaction monitoring methods with and without phosphatase treatment: Application to breast cancer signaling pathways
    • D. Domanski, L.C. Murphy, and C.H. Borchers Assay development for the determination of phosphorylation stoichiometry using multiple reaction monitoring methods with and without phosphatase treatment: application to breast cancer signaling pathways Anal. Chem. 82 2010 5610 5620
    • (2010) Anal. Chem. , vol.82 , pp. 5610-5620
    • Domanski, D.1    Murphy, L.C.2    Borchers, C.H.3
  • 24
    • 66149118232 scopus 로고    scopus 로고
    • Absolute quantification of phosphorylation on the kinase activation loop of cellular focal adhesion kinase by stable isotope dilution liquid chromatography/mass spectrometry
    • E. Ciccimaro, S.K. Hanks, K.H. Yu, and I.A. Blair Absolute quantification of phosphorylation on the kinase activation loop of cellular focal adhesion kinase by stable isotope dilution liquid chromatography/mass spectrometry Anal. Chem. 81 2009 3304 3313
    • (2009) Anal. Chem. , vol.81 , pp. 3304-3313
    • Ciccimaro, E.1    Hanks, S.K.2    Yu, K.H.3    Blair, I.A.4
  • 25
    • 78649664765 scopus 로고    scopus 로고
    • Use of selected reaction monitoring data for label-free quantification of protein modification stoichiometry
    • D. Balasubramaniam, C.L. Eissler, C.V. Stauffacher, and M.C. Hall Use of selected reaction monitoring data for label-free quantification of protein modification stoichiometry Proteomics 10 2010 4301 4305
    • (2010) Proteomics , vol.10 , pp. 4301-4305
    • Balasubramaniam, D.1    Eissler, C.L.2    Stauffacher, C.V.3    Hall, M.C.4
  • 27
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • J.R. Yates, C.I. Ruse, and A. Nakorchevsky Proteomics by mass spectrometry: Approaches, advances, and applications Annu. Rev. Biomed. Eng. 11 2009 49 79
    • (2009) Annu. Rev. Biomed. Eng. , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 28
    • 33751397720 scopus 로고    scopus 로고
    • A quantitative results-driven approach to analyzing multisite protein phosphorylation: The phosphate-dependent phosphorylation profile of the transcription factor Pho4
    • DOI 10.1074/mcp.M600238-MCP200
    • F. Zappacosta, T.S. Collingwood, M.J. Huddleston, and R.S. Annan A quantitative results-driven approach to analyzing multisite protein phosphorylation: The phosphate-dependent phosphorylation profile of the transcription factor Pho4 Mol. Cell. Proteomics 5 2006 2019 2030 (Pubitemid 44817015)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.11 , pp. 2019-2030
    • Zappacosta, F.1    Collingwood, T.S.2    Huddleston, M.J.3    Annan, R.S.4
  • 29
    • 71749117309 scopus 로고    scopus 로고
    • A peptide biosensor for detecting intracellular Abl kinase activity using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • E.A. Placzek, M.P. Plebanek, A.M. Lipchik, S.R. Kidd, and L.L. Parker A peptide biosensor for detecting intracellular Abl kinase activity using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Anal. Biochem. 397 2010 73 78
    • (2010) Anal. Biochem. , vol.397 , pp. 73-78
    • Placzek, E.A.1    Plebanek, M.P.2    Lipchik, A.M.3    Kidd, S.R.4    Parker, L.L.5
  • 30
    • 0020643218 scopus 로고
    • Measurement of chemical phosphate in proteins
    • J.E. Buss, and J.T. Stull Measurement of chemical phosphate in proteins Methods Enzymol. 99 1983 7 14 (Pubitemid 13009529)
    • (1983) Methods in Enzymology , vol.99 , pp. 7-14
    • Buss, J.E.1    Stull, J.T.2
  • 32
    • 0028273420 scopus 로고
    • Characterization and kinetic analysis of the intracellular domain of human protein tyrosine phosphatase β (HPTPβ) using synthetic phosphopeptides
    • K.W. Harder, P. Owen, L.K. Wong, R. Aebersold, I. Clark-Lewis, and F.R. Jirik Characterization and kinetic analysis of the intracellular domain of human protein tyrosine phosphatase beta (HPTP beta) using synthetic phosphopeptides Biochem. J. 298 1994 395 401 (Pubitemid 24072483)
    • (1994) Biochemical Journal , vol.298 , Issue.2 , pp. 395-401
    • Harder, K.W.1    Owen, P.2    Wong, L.K.H.3    Aebersold, R.4    Clark-Lewis, I.5    Jirik, F.R.6
  • 33
    • 33845893585 scopus 로고    scopus 로고
    • Cdk and APC activities limit the spindle-stabilizing function of Fin1 to anaphase
    • DOI 10.1038/ncb1523, PII NCB1523
    • E.L. Woodbury, and D.O. Morgan Cdk and APC activities limit the spindle-stabilizing function of Fin1 to anaphase Nat. Cell Biol. 9 2007 106 112 (Pubitemid 46024204)
    • (2007) Nature Cell Biology , vol.9 , Issue.1 , pp. 106-112
    • Woodbury, E.L.1    Morgan, D.O.2
  • 34
    • 3042822555 scopus 로고    scopus 로고
    • Getting in the ring: Proline-directed substrate specificity in the cell cycle proteins Cdc14 and CDK2-cyclinA3
    • C.H. Gray, and D. Barford Getting in the ring: Proline-directed substrate specificity in the cell cycle proteins Cdc14 and CDK2-cyclinA3 Cell Cycle 2 2003 500 502
    • (2003) Cell Cycle , vol.2 , pp. 500-502
    • Gray, C.H.1    Barford, D.2
  • 35
    • 0036323011 scopus 로고    scopus 로고
    • Disruption of centrosome structure, chromosome segregation, and cytokinesis by misexpression of human Cdc14A phosphatase
    • DOI 10.1091/mbc.01-11-0535
    • B.K. Kaiser, Z.A. Zimmerman, H. Charbonneau, and P.K. Jackson Disruption of centrosome structure, chromosome segregation, and cytokinesis by misexpression of human Cdc14A phosphatase Mol. Biol. Cell 13 2002 2289 2300 (Pubitemid 34831334)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.7 , pp. 2289-2300
    • Kaiser, B.K.1    Zimmerman, Z.A.2    Charbonneau, H.3    Jackson, P.K.4
  • 37
    • 70349546862 scopus 로고    scopus 로고
    • Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution
    • L.J. Holt, B.B. Tuch, J. Villen, A.D. Johnson, S.P. Gygi, and D.O. Morgan Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution Science 325 2009 1682 1686
    • (2009) Science , vol.325 , pp. 1682-1686
    • Holt, L.J.1    Tuch, B.B.2    Villen, J.3    Johnson, A.D.4    Gygi, S.P.5    Morgan, D.O.6
  • 40
    • 0030448251 scopus 로고    scopus 로고
    • Anaphase initiation in saccharomyces cerevisiae is controlled by the APC-dependent degradation of the anaphase inhibitor Pds1p
    • O. Cohen-Fix, J.M. Peters, M.W. Kirschner, and D. Koshland Anaphase initiation in Saccharomyces cerevisiae is controlled by the APC-dependent degradation of the anaphase inhibitor Pds1p Genes Dev. 10 1996 3081 3093 (Pubitemid 27020537)
    • (1996) Genes and Development , vol.10 , Issue.24 , pp. 3081-3093
    • Cohen-Fix, O.1    Peters, J.-M.2    Kirschner, M.W.3    Koshland, D.4
  • 41
    • 68749094119 scopus 로고    scopus 로고
    • Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics
    • P. Picotti, B. Bodenmiller, L.N. Mueller, B. Domon, and R. Aebersold Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics Cell 138 2009 795 806
    • (2009) Cell , vol.138 , pp. 795-806
    • Picotti, P.1    Bodenmiller, B.2    Mueller, L.N.3    Domon, B.4    Aebersold, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.