메뉴 건너뛰기




Volumn 12, Issue 11, 2013, Pages 3350-3359

Interrogating cAMP-dependent kinase signaling in jurkat T cells via a protein kinase A Targeted Immune-precipitation phosphoproteomics approach

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; PEPTIDE ANTIBODY; PHOSPHOPEPTIDE; PROSTAGLANDIN E2;

EID: 84887096091     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.O113.028456     Document Type: Article
Times cited : (43)

References (53)
  • 1
    • 84861897793 scopus 로고    scopus 로고
    • Mass spec trometry based proteomics and network biology
    • Bensimon, A., Heck, A. J., and Aebersold, R. (2012) Mass spectrometrybased proteomics and network biology. Annu. Rev. Biochem. 81, 379-405.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 379-405
    • Bensimon, A.1    Heck, A.J.2    Aebersold, R.3
  • 2
    • 84871297843 scopus 로고    scopus 로고
    • Next-generation proteomics: Towards an integrative view of proteome dynamics
    • Altelaar, A. F., Munoz, J., and Heck, A. J. (2012) Next-generation proteomics: Towards an integrative view of proteome dynamics. Nat. Rev. Genet. 14, 35-48.
    • (2012) Nat. Rev. Genet. , vol.14 , pp. 35-48
    • Altelaar, A.F.1    Munoz, J.2    Heck, A.J.3
  • 4
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villen, J., and Gygi, S. P. (2008) The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry. Nat. Protoc. 3, 1630-1638.
    • (2008) Nat. Protoc. , vol.3 , pp. 1630-1638
    • Villen, J.1    Gygi, S.P.2
  • 5
    • 39749186759 scopus 로고    scopus 로고
    • 2-based phosphoproteomics applied to study endogenous phosphorylation in Drosophila melanogaster
    • DOI 10.1021/pr700605z
    • Pinkse, M. W., Mohammed, S., Gouw, J. W., van Breukelen, B., Vos, H. R., and Heck, A. J. (2008) Highly robust, automated, and sensitive online TiO2-based phosphoproteomics applied to study endogenous phosphorylation in Drosophila melanogaster. J. Proteome Res. 7, 687-697. (Pubitemid 351294031)
    • (2008) Journal of Proteome Research , vol.7 , Issue.2 , pp. 687-697
    • Pinkse, M.W.H.1    Mohammed, S.2    Gouw, J.W.3    Van Breukelen, B.4    Vos, H.R.5    Heck, A.J.R.6
  • 6
    • 80054038843 scopus 로고    scopus 로고
    • Enhancing the identification of phosphopeptides from putative basophilic kinase substrates using Ti (IV) based IMAC enrichment
    • M110.006452
    • Zhou, H., Low, T. Y., Hennrich, M. L., van der Toorn, H., Schwend, T., Zou, H., Mohammed, S., and Heck, A. J. (2011) Enhancing the identification of phosphopeptides from putative basophilic kinase substrates using Ti (IV) based IMAC enrichment. Mol. Cell. Proteomics 10, M110.006452.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Zhou, H.1    Low, T.Y.2    Hennrich, M.L.3    Van Der Toorn, H.4    Schwend, T.5    Zou, H.6    Mohammed, S.7    Heck, A.J.8
  • 7
    • 36749068401 scopus 로고    scopus 로고
    • Performance characteristics of electron transfer dissociation mass spectrometry
    • DOI 10.1074/mcp.M700073-MCP200
    • Good, D. M., Wirtala, M., McAlister, G. C., and Coon, J. J. (2007) Performance characteristics of electron transfer dissociation mass spectrometry. Mol. Cell. Proteomics 6, 1942-1951. (Pubitemid 350213868)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.11 , pp. 1942-1951
    • Good, D.M.1    Wirtala, M.2    McAlister, G.C.3    Coon, J.J.4
  • 8
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications
    • Wiesner, J., Premsler, T., and Sickmann, A. (2008) Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications. Proteomics 8, 4466-4483.
    • (2008) Proteomics , vol.8 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 10
    • 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
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 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
  • 11
    • 77957703553 scopus 로고    scopus 로고
    • High-resolution mapping of prostaglandin E2-dependent signaling networks identifies a constitutively active PKA signaling node in CD8-CD45RO- T cells
    • Oberprieler, N. G., Lemeer, S., Kalland, M. E., Torgersen, K. M., Heck, A. J., and Tasken, K. (2010) High-resolution mapping of prostaglandin E2-dependent signaling networks identifies a constitutively active PKA signaling node in CD8-CD45RO- T cells. Blood 116, 2253-2265.
    • (2010) Blood , vol.116 , pp. 2253-2265
    • Oberprieler, N.G.1    Lemeer, S.2    Kalland, M.E.3    Torgersen, K.M.4    Heck, A.J.5    Tasken, K.6
  • 12
    • 70350462371 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions
    • Mayya, V., Lundgren, D. H., Hwang, S. I., Rezaul, K., Wu, L., Eng, J. K., Rodionov, V., and Han, D. K. (2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal. 2, ra46.
    • (2009) Sci. Signal. , vol.2
    • Mayya, V.1    Lundgren, D.H.2    Hwang, S.I.3    Rezaul, K.4    Wu, L.5    Eng, J.K.6    Rodionov, V.7    Han, D.K.8
  • 14
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • DOI 10.1021/ac0498617
    • Pinkse, M. W., Uitto, P. M., Hilhorst, M. J., Ooms, B., and Heck, A. J. (2004) Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-nanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 76, 3935-3943. (Pubitemid 38943662)
    • (2004) Analytical Chemistry , vol.76 , Issue.14 , pp. 3935-3943
    • Pinkse, M.W.H.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.R.5
  • 15
    • 41149110237 scopus 로고    scopus 로고
    • Electrostatic repulsion hydrophilic interaction chromatography for isocratic separation of charged solutes and selective isolation of phosphopeptides
    • DOI 10.1021/ac070997p
    • Alpert, A. J. (2008) Electrostatic repulsion hydrophilic interaction chromatography for isocratic separation of charged solutes and selective isolation of phosphopeptides. Anal. Chem. 80, 62-76. (Pubitemid 351448406)
    • (2008) Analytical Chemistry , vol.80 , Issue.1 , pp. 62-76
    • Alpert, A.J.1
  • 16
    • 80052469143 scopus 로고    scopus 로고
    • Development and application of a phosphoproteomic method using electrostatic repulsionhydrophilic interaction chromatography (ERLIC), IMAC, and LC-MS/MS analysis to study Marek's Disease Virus infection
    • Chien, K. Y., Liu, H. C., and Goshe, M. B. (2011) Development and application of a phosphoproteomic method using electrostatic repulsionhydrophilic interaction chromatography (ERLIC), IMAC, and LC-MS/MS analysis to study Marek's Disease Virus infection. J. Proteome Res. 10, 4041-4053.
    • (2011) J. Proteome Res. , vol.10 , pp. 4041-4053
    • Chien, K.Y.1    Liu, H.C.2    Goshe, M.B.3
  • 17
    • 43849091451 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection
    • DOI 10.1074/mcp.M700543-MCP200
    • McNulty, D. E., and Annan, R. S. (2008) Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection. Mol. Cell. Proteomics 7, 971-980. (Pubitemid 351737096)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.5 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 19
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • DOI 10.1074/mcp.M500089-MCP200
    • Zhang, Y., Wolf-Yadlin, A., Ross, P. L., Pappin, D. J., Rush, J., Lauffenburger, D. A., and White, F. M. (2005) Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol. Cell. Proteomics 4, 1240-1250. (Pubitemid 41448712)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4    Rush, J.5    Lauffenburger, D.A.6    White, F.M.7
  • 20
    • 76649110554 scopus 로고    scopus 로고
    • In-depth qualitative and quantitative profiling of tyrosine phosphorylation using a combination of phosphopeptide immunoaffinity purification and stable isotope dimethyl labeling
    • Boersema, P. J., Foong, L. Y., Ding, V. M., Lemeer, S., van Breukelen, B., Philp, R., Boekhorst, J., Snel, B., den Hertog, J., Choo, A. B., and Heck, A. J. (2010) In-depth qualitative and quantitative profiling of tyrosine phosphorylation using a combination of phosphopeptide immunoaffinity purification and stable isotope dimethyl labeling. Mol. Cell. Proteomics 9, 84-99.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 84-99
    • Boersema, P.J.1    Foong, L.Y.2    Ding, V.M.3    Lemeer, S.4    Van Breukelen, B.5    Philp, R.6    Boekhorst, J.7    Snel, B.8    Den Hertog, J.9    Choo, A.B.10    Heck, A.J.11
  • 26
    • 34748916981 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: A critical review
    • DOI 10.1007/s00216-007-1486-6, Proteomics/Molecular Imaging
    • Bantscheff, M., Schirle, M., Sweetman, G., Rick, J., and Kuster, B. (2007) Quantitative mass spectrometry in proteomics: A critical review. Anal. Bioanal. Chem. 389, 1017-1031. (Pubitemid 47482251)
    • (2007) Analytical and Bioanalytical Chemistry , vol.389 , Issue.4 , pp. 1017-1031
    • Bantscheff, M.1    Schirle, M.2    Sweetman, G.3    Rick, J.4    Kuster, B.5
  • 28
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema, P. J., Raijmakers, R., Lemeer, S., Mohammed, S., and Heck, A. J. (2009) Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat. Protoc. 4, 484-494.
    • (2009) Nat. Protoc. , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 29
    • 0348014635 scopus 로고    scopus 로고
    • Stable-isotope dimethyl labeling for quantitative proteomics
    • Hsu, J. L., Huang, S. Y., Chow, N. H., and Chen, S. H. (2003) Stable-isotope dimethyl labeling for quantitative proteomics. Anal. Chem. 75, 6843-6852.
    • (2003) Anal. Chem. , vol.75 , pp. 6843-6852
    • Hsu, J.L.1    Huang, S.Y.2    Chow, N.H.3    Chen, S.H.4
  • 30
    • 0029165737 scopus 로고
    • Determination of cyclic nucleotide-dependent protein kinase substrate specificity by the use of peptide libraries on cellulose paper
    • Tegge, W., Frank, R., Hofmann, F., and Dostmann, W. R. (1995) Determination of cyclic nucleotide-dependent protein kinase substrate specificity by the use of peptide libraries on cellulose paper. Biochemistry 34, 10569-10577.
    • (1995) Biochemistry , vol.34 , pp. 10569-10577
    • Tegge, W.1    Frank, R.2    Hofmann, F.3    Dostmann, W.R.4
  • 31
    • 0035413602 scopus 로고    scopus 로고
    • Physiological substrates of cAMP-dependent protein kinase
    • DOI 10.1021/cr000236l
    • Shabb, J. B. (2001) Physiological substrates of cAMP-dependent protein kinase. Chem. Rev. 101, 2381-2411. (Pubitemid 35373025)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2381-2411
    • Shabb, J.B.1
  • 33
    • 79953681012 scopus 로고    scopus 로고
    • Antibody-free peptide substrate screening of serine/threonine kinase (protein kinase A) with a biotinylated detection probe
    • Kim, M., Park, Y. S., Shin, D. S., Kim, J., Kim, B. G., and Lee, Y. S. (2011) Antibody-free peptide substrate screening of serine/threonine kinase (protein kinase A) with a biotinylated detection probe. Anal. Bio chem. 413, 30-35.
    • (2011) Anal. Bio Chem. , vol.413 , pp. 30-35
    • Kim, M.1    Park, Y.S.2    Shin, D.S.3    Kim, J.4    Kim, B.G.5    Lee, Y.S.6
  • 34
    • 79960821208 scopus 로고    scopus 로고
    • Discovery of cellular substrates for protein kinase A using a peptide array screening protocol
    • Smith, F. D., Samelson, B. K., and Scott, J. D. (2011) Discovery of cellular substrates for protein kinase A using a peptide array screening protocol. Bio chem. J. 438, 103-110.
    • (2011) Bio Chem. J. , vol.438 , pp. 103-110
    • Smith, F.D.1    Samelson, B.K.2    Scott, J.D.3
  • 35
    • 56149086397 scopus 로고    scopus 로고
    • Decision tree-driven tandem mass spectrometry for shotgun proteomics
    • Swaney, D. L., McAlister, G. C., and Coon, J. J. (2008) Decision tree-driven tandem mass spectrometry for shotgun proteomics. Nat. Methods 5, 959-964.
    • (2008) Nat. Methods , vol.5 , pp. 959-964
    • Swaney, D.L.1    McAlister, G.C.2    Coon, J.J.3
  • 36
    • 84855361145 scopus 로고    scopus 로고
    • Regulation of immune responses by prostaglandin E2
    • Kalinski, P. (2012) Regulation of immune responses by prostaglandin E2. J. Immunol. 188, 21-28.
    • (2012) J. Immunol. , vol.188 , pp. 21-28
    • Kalinski, P.1
  • 37
    • 31544464331 scopus 로고    scopus 로고
    • + T cell activation by inhibition of lck: Implications in Hodgkin's lymphoma
    • DOI 10.1158/0008-5472.CAN-05-3252
    • Chemnitz, J. M., Driesen, J., Classen, S., Riley, J. L., Debey, S., Beyer, M., Popov, A., Zander, T., and Schultze, J. L. (2006) Prostaglandin E2 impairs CD4- T cell activation by inhibition of lck: implications in Hodgkin's lymphoma. Cancer Res. 66, 1114-1122. (Pubitemid 43165980)
    • (2006) Cancer Research , vol.66 , Issue.2 , pp. 1114-1122
    • Chemnitz, J.M.1    Driesen, J.2    Classen, S.3    Riley, J.L.4    Debey, S.5    Beyer, M.6    Popov, A.7    Zander, T.8    Schultze, J.L.9
  • 42
    • 84857047339 scopus 로고    scopus 로고
    • Phospho site plus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B., Skrzypek, E., Murray, B., Latham, V., and Sullivan, M. (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.
    • (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    Latham, V.7    Sullivan, M.8
  • 44
    • 84863727431 scopus 로고    scopus 로고
    • Prostaglandin E2 and T cells: Friends or foes?
    • Sreeramkumar, V., Fresno, M., and Cuesta, N. (2012) Prostaglandin E2 and T cells: friends or foes? Immunol. Cell Biol. 90, 579-586.
    • (2012) Immunol. Cell Biol. , vol.90 , pp. 579-586
    • Sreeramkumar, V.1    Fresno, M.2    Cuesta, N.3
  • 48
    • 0035798567 scopus 로고    scopus 로고
    • Phosphorylation of the integrin alpha 4 cytoplasmic domain regulates paxillin binding
    • Han, J., Liu, S., Rose, D. M., Schlaepfer, D. D., McDonald, H., and Ginsberg, M. H. (2001) Phosphorylation of the integrin alpha 4 cytoplasmic domain regulates paxillin binding. J. Biol. Chem. 276, 40903-40909.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40903-40909
    • Han, J.1    Liu, S.2    Rose, D.M.3    Schlaepfer, D.D.4    McDonald, H.5    Ginsberg, M.H.6
  • 49
    • 0033539801 scopus 로고    scopus 로고
    • 4 integrins modifies integrin-dependent biological responses
    • Liu, S., Thomas, S. M., Woodside, D. G., Rose, D. M., Kiosses, W. B., Pfaff, M., and Ginsberg, M. H. (1999) Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses. Nature 402, 676-681. (Pubitemid 129516339)
    • (1999) Nature , vol.402 , Issue.6762 , pp. 676-681
    • Liu, S.1    Thomas, S.M.2    Woodside, D.G.3    Rose, D.M.4    Klosses, W.B.5    Pfaff, M.6    Ginsberg, M.H.7
  • 51
    • 0030857296 scopus 로고    scopus 로고
    • Phosphorylation of ATF-1 enhances its DNA binding and transcription of the Na,K-ATPase α1 subunit gene promoter
    • DOI 10.1093/nar/25.4.877
    • Kobayashi, M., Shimomura, A., Hagiwara, M., and Kawakami, K. (1997) Phosphorylation of ATF-1 enhances its DNA binding and transcription of the Na, K-ATPase alpha 1 subunit gene promoter. Nucleic Acids Res. 25, 877-882. (Pubitemid 27299847)
    • (1997) Nucleic Acids Research , vol.25 , Issue.4 , pp. 877-882
    • Kobayashi, M.1    Shimomura, A.2    Hagiwara, M.3    Kawakami, K.4
  • 52
    • 54749124446 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 3-mediated activating transcription factor 1 phosphorylation enhances cell transformation
    • Zheng, D., Cho, Y. Y., Lau, A. T., Zhang, J., Ma, W. Y., Bode, A. M., and Dong, Z. (2008) Cyclin-dependent kinase 3-mediated activating transcription factor 1 phosphorylation enhances cell transformation. Cancer Res. 68, 7650-7660.
    • (2008) Cancer Res. , vol.68 , pp. 7650-7660
    • Zheng, D.1    Cho, Y.Y.2    Lau, A.T.3    Zhang, J.4    Ma, W.Y.5    Bode, A.M.6    Dong, Z.7
  • 53
    • 79952695731 scopus 로고    scopus 로고
    • Cyclic AMP-mediated immune regulation- overview of mechanisms of action in T cells
    • Mosenden, R., and Tasken, K. (2011) Cyclic AMP-mediated immune regulation- overview of mechanisms of action in T cells. Cell. Signal. 23, 1009-1016.
    • (2011) Cell. Signal , vol.23 , pp. 1009-1016
    • Mosenden, R.1    Tasken, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.