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Volumn 12, Issue 5, 2013, Pages 1395-1406

Isotope coded protein labeling coupled immunoprecipitation (icpl-ip): A novel approach for quantitative protein complex analysis from native tissue

Author keywords

[No Author keywords available]

Indexed keywords

BETA TUBULIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 84877631042     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.O112.023648     Document Type: Article
Times cited : (6)

References (55)
  • 1
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • DOI 10.1038/13732
    • Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., and Séraphin, B. (1999) A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032 (Pubitemid 29474865)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 2
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • DOI 10.1006/meth.2001.1183
    • Puig, O., Caspary, F., Rigaut, G., Rutz, B., Bouveret, E., Bragado-Nilsson, E., Wilm, M., and Séraphin, B. (2001) The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods 24, 218-229 (Pubitemid 32846428)
    • (2001) Methods , vol.24 , Issue.3 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6    Wilm, M.7    Seraphin, B.8
  • 3
    • 33751230224 scopus 로고    scopus 로고
    • Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK)
    • DOI 10.1038/nmeth972, PII NMETH972
    • Selbach, M., and Mann, M. (2006) Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK). Nat. Methods 3, 981-983 (Pubitemid 44782696)
    • (2006) Nature Methods , vol.3 , Issue.12 , pp. 981-983
    • Selbach, M.1    Mann, M.2
  • 4
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (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
    • (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    Mann, M.7
  • 5
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., and Mann, M. (2005) Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1, 252-262
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 6
    • 77952226764 scopus 로고    scopus 로고
    • Super-SILAC mix for quantitative proteomics of human tumor tissue
    • Geiger, T., Cox, J., Ostasiewicz, P., Wisniewski, J. R., and Mann, M. (2010) Super-SILAC mix for quantitative proteomics of human tumor tissue. Nat. Methods 7, 383-385
    • (2010) Nat. Methods , vol.7 , pp. 383-385
    • Geiger, T.1    Cox, J.2    Ostasiewicz, P.3    Wisniewski, J.R.4    Mann, M.5
  • 8
    • 47549099572 scopus 로고    scopus 로고
    • SILAC Mouse for Quantitative Proteomics Uncovers Kindlin-3 as an Essential Factor for Red Blood Cell Function
    • DOI 10.1016/j.cell.2008.05.033, PII S0092867408006958
    • Krüger, M., Moser, M., Ussar, S., Thievessen, I., Luber, C. A., Forner, F., Schmidt, S., Zanivan, S., Fässler, R., and Mann, M. (2008) SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 134, 353-364 (Pubitemid 352010327)
    • (2008) Cell , vol.134 , Issue.2 , pp. 353-364
    • Kruger, M.1    Moser, M.2    Ussar, S.3    Thievessen, I.4    Luber, C.A.5    Forner, F.6    Schmidt, S.7    Zanivan, S.8    Fassler, R.9    Mann, M.10
  • 9
    • 34548391374 scopus 로고    scopus 로고
    • Quantification of the synaptosomal proteome of the rat cerebellum during post-natal development
    • DOI 10.1101/gr.6375007
    • McClatchy, D. B., Liao, L., Park, S. K., Venable, J. D., and Yates, J. R. (2007) Quantification of the synaptosomal proteome of the rat cerebellum during post-natal development. Genome Res. 17, 1378-1388 (Pubitemid 47360912)
    • (2007) Genome Research , vol.17 , Issue.9 , pp. 1378-1388
    • McClatchy, D.B.1    Liao, L.2    Sung, K.P.3    Venable, J.D.4    Yates, J.R.5
  • 10
    • 13244260803 scopus 로고    scopus 로고
    • A novel strategy for quantitative proteomics using isotope-coded protein labels
    • DOI 10.1002/pmic.200400873
    • Schmidt, A., Kellermann, J., and Lottspeich, F. (2005) A novel strategy for quantitative proteomics using isotope-coded protein labels. Proteomics 5, 4-15 (Pubitemid 40189632)
    • (2005) Proteomics , vol.5 , Issue.1 , pp. 4-15
    • Schmidt, A.1    Kellermann, J.2    Lottspeich, F.3
  • 11
    • 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 (Pubitemid 350250468)
    • (2007) Proteomics , vol.7 , Issue.23 , pp. 4228-4234
    • Gloeckner, C.J.1    Boldt, K.2    Schumacher, A.3    Roepman, R.4    Ueffing, M.5
  • 13
    • 0035699391 scopus 로고    scopus 로고
    • Identification of novel molecular components of the photoreceptor connecting cilium by immunoscreens
    • DOI 10.1006/exer.2001.1086
    • Schmitt, A., and Wolfrum, U. (2001) Identification of novel molecular components of the photoreceptor connecting cilium by immunoscreens. Exp. Eye Res. 73, 837-849 (Pubitemid 34112109)
    • (2001) Experimental Eye Research , vol.73 , Issue.6 , pp. 837-849
    • Schmitt, A.1    Wolfrum, U.2
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 33645774852 scopus 로고    scopus 로고
    • Modular stop and go extraction tips with stacked disks for parallel and multidimensional Peptide fractionation in proteomics
    • Ishihama, Y., Rappsilber, J., and Mann, M. (2006) Modular stop and go extraction tips with stacked disks for parallel and multidimensional Peptide fractionation in proteomics. J. Proteome Res. 5, 988-994
    • (2006) J. Proteome Res. , vol.5 , pp. 988-994
    • Ishihama, Y.1    Rappsilber, J.2    Mann, M.3
  • 16
    • 0037317228 scopus 로고    scopus 로고
    • Stop And Go Extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • DOI 10.1021/ac026117i
    • Rappsilber, J., Ishihama, Y., and Mann, M. (2003) Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 75, 663-670 (Pubitemid 36176744)
    • (2003) Analytical Chemistry , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 19
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • 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
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 23
    • 0028117919 scopus 로고
    • Purification and characterization of ensconsin, a novel microtubule stabilizing protein
    • Bulinski, J. C., and Bossler, A. (1994) Purification and characterization of ensconsin, a novel microtubule stabilizing protein. J. Cell Sci. 107 (Pt 10), 2839-2849 (Pubitemid 24340904)
    • (1994) Journal of Cell Science , vol.107 , Issue.10 , pp. 2839-2849
    • Bulinski, J.C.1    Bossler, A.2
  • 24
    • 46749110073 scopus 로고    scopus 로고
    • Proteomics of photoreceptor outer segments identifies a subset of SNARE and rab proteins implicated in membrane vesicle trafficking and fusion
    • DOI 10.1074/mcp.M700571-MCP200
    • Kwok, M. C., Holopainen, J. M., Molday, L. L., Foster, L. J., and Molday, R. S. (2008) Proteomics of photoreceptor outer segments identifies a subset of SNARE and Rab proteins implicated in membrane vesicle trafficking and fusion. Mol. Cell. Proteomics 7, 1053-1066 (Pubitemid 351943953)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.6 , pp. 1053-1066
    • Kwok, M.C.M.1    Holopainen, J.M.2    Molday, L.L.3    Fosteer, L.J.4    Molday, R.S.5
  • 25
    • 33750359913 scopus 로고    scopus 로고
    • Light-driven translocation of signaling proteins in vertebrate photoreceptors
    • DOI 10.1016/j.tcb.2006.09.001, PII S0962892406002376
    • Calvert, P. D., Strissel, K. J., Schiesser, W. E., Pugh, E. N., Jr., and Arshavsky, V. Y. (2006) Light-driven translocation of signaling proteins in vertebrate photoreceptors. Trends Cell Biol. 16, 560-568 (Pubitemid 44636215)
    • (2006) Trends in Cell Biology , vol.16 , Issue.11 , pp. 560-568
    • Calvert, P.D.1    Strissel, K.J.2    Schiesser, W.E.3    Pugh Jr., E.N.4    Arshavsky, V.Y.5
  • 27
    • 40849108777 scopus 로고    scopus 로고
    • Mapping the integrin-linked kinase interactome using SILAC
    • Dobreva, I., Fielding, A., Foster, L. J., and Dedhar, S. (2008) Mapping the integrin-linked kinase interactome using SILAC. J. Proteome Res. 7, 1740-1749
    • (2008) J. Proteome Res. , vol.7 , pp. 1740-1749
    • Dobreva, I.1    Fielding, A.2    Foster, L.J.3    Dedhar, S.4
  • 29
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998) Rho GTPases and the actin cytoskeleton. Science 279, 509-514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 30
    • 0030267458 scopus 로고    scopus 로고
    • Rho: Theme and variations
    • Ridley, A. J. (1996) Rho: theme and variations. Current Biol. 6, 1256-1264
    • (1996) Current Biol. , vol.6 , pp. 1256-1264
    • Ridley, A.J.1
  • 31
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and Hall, A. (1992) The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 32
    • 4243066292 scopus 로고    scopus 로고
    • Botulinum toxin type A targets RhoB to inhibit lysophosphatidic acid-stimulated actin reorganization and acetylcholine release in nerve growth factor-treated PC12 cells
    • DOI 10.1124/jpet.104.065318
    • Ishida, H., Zhang, X., Erickson, K., and Ray, P. (2004) Botulinum toxin type A targets RhoB to inhibit lysophosphatidic acid-stimulated actin reorganization and acetylcholine release in nerve growth factor-treated PC12 cells. J. Pharmacol. Exp. Ther. 310, 881-889 (Pubitemid 39108907)
    • (2004) Journal of Pharmacology and Experimental Therapeutics , vol.310 , Issue.3 , pp. 881-889
    • Ishida, H.1    Zhang, X.2    Erickson, K.3    Ray, P.4
  • 34
    • 0028933716 scopus 로고
    • Ultrastructural localization of ras-related proteins using epitope-tagged plasmids
    • Robertson, D., Paterson, H. F., Adamson, P., Hall, A., and Monaghan, P. (1995) Ultrastructural localization of ras-related proteins using epitope-tagged plasmids. J. Histochem. Cytochem. 43, 471-480
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 471-480
    • Robertson, D.1    Paterson, H.F.2    Adamson, P.3    Hall, A.4    Monaghan, P.5
  • 36
    • 0036468982 scopus 로고    scopus 로고
    • The oncoprotein 18/stathmin family of microtubule destabilizers
    • Cassimeris, L. (2002) The oncoprotein 18/stathmin family of microtubule destabilizers. Curr. Opin. Cell Biol. 14, 18-24
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 18-24
    • Cassimeris, L.1
  • 37
    • 0346750741 scopus 로고    scopus 로고
    • Role of the Microtubule Destabilizing Proteins SCG10 and Stathmin in Neuronal Growth
    • DOI 10.1002/neu.10279
    • Grenningloh, G., Soehrman, S., Bondallaz, P., Ruchti, E., and Cadas, H. (2004) Role of the microtubule destabilizing proteins SCG10 and stathmin in neuronal growth. J. Neurobiol. 58, 60-69 (Pubitemid 37543338)
    • (2004) Journal of Neurobiology , vol.58 , Issue.1 , pp. 60-69
    • Grenningloh, G.1    Soehrman, S.2    Bondallaz, P.3    Ruchti, E.4    Cadas, H.5
  • 38
    • 0028556361 scopus 로고
    • Molecular cloning of two small GTP-binding proteins from human skeletal muscle
    • Zhu, A. X., Zhao, Y., and Flier, J. S. (1994) Molecular cloning of two small GTP-binding proteins from human skeletal muscle. Biochem. Biophys. Res. Commun. 205, 1875-1882
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1875-1882
    • Zhu, A.X.1    Zhao, Y.2    Flier, J.S.3
  • 39
    • 1042278142 scopus 로고    scopus 로고
    • A Novel Actin-bundling Kinesin-related Protein from Dictyostelium discoideum
    • DOI 10.1074/jbc.M308022200
    • Iwai, S., Ishiji, A., Mabuchi, I., and Sutoh, K. (2004) A novel actin-bundling kinesin-related protein from Dictyostelium discoideum. J. Biol. Chem. 279, 4696-4704 (Pubitemid 38199063)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4696-4704
    • Iwai, S.1    Ishiji, A.2    Mabuchi, I.3    Sutoh, K.4
  • 40
    • 0031769401 scopus 로고    scopus 로고
    • Association of kinesin with microtubules in diverse cytoskeletal systems in the outer segments of rods and cones
    • Eckmiller, M. S., and Toman, A. (1998) Association of kinesin with microtubules in diverse cytoskeletal systems in the outer segments of rods and cones. Acta Anatomica 162, 133-141 (Pubitemid 28550597)
    • (1998) Acta Anatomica , vol.162 , Issue.2-3 , pp. 133-141
    • Eckmiller, M.S.1
  • 41
    • 0033983938 scopus 로고    scopus 로고
    • Regulation of endocytic traffic by Rho family GTPases
    • DOI 10.1016/S0962-8924(99)01710-9, PII S0962892499017109
    • Ellis, S., and Mellor, H. (2000) Regulation of endocytic traffic by rho family GTPases. Trends Cell Biol. 10, 85-88 (Pubitemid 30110689)
    • (2000) Trends in Cell Biology , vol.10 , Issue.3 , pp. 85-88
    • Ellis, S.1    Mellor, H.2
  • 42
    • 33644838018 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: New insights into caveolae and non-caveolar lipid raft carriers
    • Kirkham, M., and Parton, R. G. (2005) Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers. Biochim. Biophys. Acta 1746, 349-363
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 349-363
    • Kirkham, M.1    Parton, R.G.2
  • 43
    • 0242268532 scopus 로고    scopus 로고
    • Lipid rafts and caveolae as portals for endocytosis: New insights and common mechanisms
    • DOI 10.1034/j.1600-0854.2003.00128.x
    • Parton, R. G., and Richards, A. A. (2003) Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms. Traffic 4, 724-738 (Pubitemid 37361854)
    • (2003) Traffic , vol.4 , Issue.11 , pp. 724-738
    • Parton, R.G.1    Richards, A.A.2
  • 44
    • 0026612457 scopus 로고
    • Intracellular localization of the P21rho proteins
    • Adamson, P., Paterson, H. F., and Hall, A. (1992) Intracellular localization of the P21rho proteins. J. Cell Biol. 119, 617-627
    • (1992) J. Cell Biol. , vol.119 , pp. 617-627
    • Adamson, P.1    Paterson, H.F.2    Hall, A.3
  • 46
    • 78650795916 scopus 로고    scopus 로고
    • Cellular expression and subcellular localization of secretogranin II in the mouse hippocampus and cerebellum
    • Miyazaki, T., Yamasaki, M., Uchigashima, M., Matsushima, A., and Watanabe, M. (2011) Cellular expression and subcellular localization of secretogranin II in the mouse hippocampus and cerebellum. Eur. J. Neurosci. 33, 82-94
    • (2011) Eur. J. Neurosci. , vol.33 , pp. 82-94
    • Miyazaki, T.1    Yamasaki, M.2    Uchigashima, M.3    Matsushima, A.4    Watanabe, M.5
  • 48
    • 80051675515 scopus 로고    scopus 로고
    • Tetrahydrobiopterin: Biochemistry and pathophysiology
    • Werner, E. R., Blau, N., and Thöny, B. (2011) Tetrahydrobiopterin: biochemistry and pathophysiology. Biochem. J. 438, 397-414
    • (2011) Biochem. J. , vol.438 , pp. 397-414
    • Werner, E.R.1    Blau, N.2    Thöny, B.3
  • 50
    • 0021710353 scopus 로고
    • Interaction of tubulin with chromatin proteins. H1 and core histones
    • Mithieux, G., Alquier, C., Roux, B., and Rousset, B. (1984) Interaction of tubulin with chromatin proteins. H1 and core histones. J. Biol. Chem. 259, 15523-15531 (Pubitemid 15190768)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.24 , pp. 15523-15531
    • Mithieux, G.1    Alquier, C.2    Roux, B.3    Rousset, B.4
  • 51
    • 0026478027 scopus 로고
    • Stabilization of sea urchin flagellar microtubules by histone H1
    • Multigner, L., Gagnon, J., Van Dorsselaer, A., and Job, D. (1992) Stabilization of sea urchin flagellar microtubules by histone H1. Nature 360, 33-39
    • (1992) Nature , vol.360 , pp. 33-39
    • Multigner, L.1    Gagnon, J.2    Van Dorsselaer, A.3    Job, D.4
  • 52
    • 65149084160 scopus 로고    scopus 로고
    • The AAA+ superfamily of functionally diverse proteins
    • Snider, J., Thibault, G., and Houry, W. A. (2008) The AAA+ superfamily of functionally diverse proteins. Genome Biol. 9, 216
    • (2008) Genome Biol. , vol.9 , pp. 216
    • Snider, J.1    Thibault, G.2    Houry, W.A.3
  • 53
    • 0034194659 scopus 로고    scopus 로고
    • Molecular cloning of a novel membrane glycoprotein, pal, specifically expressed in photoreceptor cells of the retina and containing leucine-rich repeat
    • Gomi, F., Imaizumi, K., Yoneda, T., Taniguchi, M., Mori, Y., Miyoshi, K., Hitomi, J., Fujikado, T., Tano, Y., and Tohyama, M. (2000) Molecular cloning of a novel membrane glycoprotein, pal, specifically expressed in photoreceptor cells of the retina and containing leucine-rich repeat. J. Neurosci. 20, 3206-3213 (Pubitemid 30263138)
    • (2000) Journal of Neuroscience , vol.20 , Issue.9 , pp. 3206-3213
    • Gomi, F.1    Imaizumi, K.2    Yoneda, T.3    Taniguchi, M.4    Mori, Y.5    Miyoshi, K.6    Hitomi, J.7    Fujikado, T.8    Tano, Y.9    Tohyama, M.10
  • 54
    • 0014077497 scopus 로고
    • The renewal of photoreceptor cell outer segments
    • Young, R. W. (1967) The renewal of photoreceptor cell outer segments. J. Cell Biol. 33, 61-72
    • (1967) J. Cell Biol. , vol.33 , pp. 61-72
    • Young, R.W.1
  • 55
    • 0026635452 scopus 로고
    • Morphogenesis of the photoreceptor outer segment during postnatal development in the mouse (BALB/c) retina
    • Obata, S., and Usukura, J. (1992) Morphogenesis of the photoreceptor outer segment during postnatal development in the mouse (BALB/c) retina. Cell Tissue Res. 269, 39-48
    • (1992) Cell Tissue Res. , vol.269 , pp. 39-48
    • Obata, S.1    Usukura, J.2


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