메뉴 건너뛰기




Volumn 3, Issue 2, 2013, Pages 552-566

In Vivo SILAC-Based Proteomics Reveals Phosphoproteome Changes during Mouse Skin Carcinogenesis

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; P21 ACTIVATED KINASE 4; PROTEIN KINASE C;

EID: 84874259874     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2013.01.003     Document Type: Article
Times cited : (88)

References (66)
  • 1
    • 70249123827 scopus 로고    scopus 로고
    • Multi-stage chemical carcinogenesis in mouse skin: fundamentals and applications
    • Abel E.L., Angel J.M., Kiguchi K., DiGiovanni J. Multi-stage chemical carcinogenesis in mouse skin: fundamentals and applications. Nat. Protoc. 2009, 4:1350-1362.
    • (2009) Nat. Protoc. , vol.4 , pp. 1350-1362
    • Abel, E.L.1    Angel, J.M.2    Kiguchi, K.3    DiGiovanni, J.4
  • 5
    • 0035907296 scopus 로고    scopus 로고
    • The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity
    • Chong C., Tan L., Lim L., Manser E. The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity. J. Biol. Chem. 2001, 276:17347-17353.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17347-17353
    • Chong, C.1    Tan, L.2    Lim, L.3    Manser, E.4
  • 7
    • 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., Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 2008, 26:1367-1372.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 10
    • 0026729695 scopus 로고
    • Multistage carcinogenesis in mouse skin
    • DiGiovanni J. Multistage carcinogenesis in mouse skin. Pharmacol. Ther. 1992, 54:63-128.
    • (1992) Pharmacol. Ther. , vol.54 , pp. 63-128
    • DiGiovanni, J.1
  • 14
    • 79551663189 scopus 로고    scopus 로고
    • Use of stable isotope labeling by amino acids in cell culture as a spike-in standard in quantitative proteomics
    • Geiger T., Wisniewski J.R., Cox J., Zanivan S., Kruger M., Ishihama Y., Mann M. Use of stable isotope labeling by amino acids in cell culture as a spike-in standard in quantitative proteomics. Nat. Protoc. 2011, 6:147-157.
    • (2011) Nat. Protoc. , vol.6 , pp. 147-157
    • Geiger, T.1    Wisniewski, J.R.2    Cox, J.3    Zanivan, S.4    Kruger, M.5    Ishihama, Y.6    Mann, M.7
  • 15
    • 0023755783 scopus 로고
    • Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity
    • Gould K.L., Hunter T. Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity. Mol. Cell. Biol. 1988, 8:3345-3356.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3345-3356
    • Gould, K.L.1    Hunter, T.2
  • 16
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D., Weinberg R.A. Hallmarks of cancer: the next generation. Cell 2011, 144:646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 17
    • 77955976922 scopus 로고    scopus 로고
    • The grand challenge to decipher the cancer proteome
    • Hanash S., Taguchi A. The grand challenge to decipher the cancer proteome. Nat. Rev. Cancer 2010, 10:652-660.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 652-660
    • Hanash, S.1    Taguchi, A.2
  • 18
    • 78349310118 scopus 로고    scopus 로고
    • Phosphoproteomics in cancer
    • Harsha H.C., Pandey A. Phosphoproteomics in cancer. Mol. Oncol. 2010, 4:482-495.
    • (2010) Mol. Oncol. , vol.4 , pp. 482-495
    • Harsha, H.C.1    Pandey, A.2
  • 19
    • 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
    • Hornbeck P.V., Kornhauser J.M., Tkachev S., Zhang B., Skrzypek E., Murray B., Latham V., Sullivan M. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 2012, 40(Database issue):D261-D270.
    • (2012) Nucleic Acids Res. , vol.40 , Issue.DATABASE ISSUE
    • 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
  • 20
    • 30044447771 scopus 로고    scopus 로고
    • Identification of novel tumour-associated genes differentially expressed in the process of squamous cell cancer development
    • Hummerich L., Müller R., Hess J., Kokocinski F., Hahn M., Fürstenberger G., Mauch C., Lichter P., Angel P. Identification of novel tumour-associated genes differentially expressed in the process of squamous cell cancer development. Oncogene 2006, 25:111-121.
    • (2006) Oncogene , vol.25 , pp. 111-121
    • Hummerich, L.1    Müller, R.2    Hess, J.3    Kokocinski, F.4    Hahn, M.5    Fürstenberger, G.6    Mauch, C.7    Lichter, P.8    Angel, P.9
  • 23
    • 0242708723 scopus 로고    scopus 로고
    • Expression of desmosomal proteins in squamous cell carcinomas of the skin
    • Kurzen H., Münzing I., Hartschuh W. Expression of desmosomal proteins in squamous cell carcinomas of the skin. J. Cutan. Pathol. 2003, 30:621-630.
    • (2003) J. Cutan. Pathol. , vol.30 , pp. 621-630
    • Kurzen, H.1    Münzing, I.2    Hartschuh, W.3
  • 24
    • 23444434936 scopus 로고    scopus 로고
    • Gene expression profiling of cancer progression reveals intrinsic regulation of transforming growth factor-beta signaling in ErbB2/Neu-induced tumors from transgenic mice
    • Landis M.D., Seachrist D.D., Montañez-Wiscovich M.E., Danielpour D., Keri R.A. Gene expression profiling of cancer progression reveals intrinsic regulation of transforming growth factor-beta signaling in ErbB2/Neu-induced tumors from transgenic mice. Oncogene 2005, 24:5173-5190.
    • (2005) Oncogene , vol.24 , pp. 5173-5190
    • Landis, M.D.1    Seachrist, D.D.2    Montañez-Wiscovich, M.E.3    Danielpour, D.4    Keri, R.A.5
  • 25
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen M.R., Thingholm T.E., Jensen O.N., Roepstorff P., Jørgensen T.J. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 2005, 4:873-886.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jørgensen, T.J.5
  • 27
    • 75649110495 scopus 로고    scopus 로고
    • MT1-MMP controls human mesenchymal stem cell trafficking and differentiation
    • Lu C., Li X.Y., Hu Y., Rowe R.G., Weiss S.J. MT1-MMP controls human mesenchymal stem cell trafficking and differentiation. Blood 2010, 115:221-229.
    • (2010) Blood , vol.115 , pp. 221-229
    • Lu, C.1    Li, X.Y.2    Hu, Y.3    Rowe, R.G.4    Weiss, S.J.5
  • 28
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann M. Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 2006, 7:952-958.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 952-958
    • Mann, M.1
  • 29
    • 50849107639 scopus 로고    scopus 로고
    • Signal transduction in transgenic mouse models of human breast cancer-implications for human breast cancer
    • Marcotte R., Muller W.J. Signal transduction in transgenic mouse models of human breast cancer-implications for human breast cancer. J. Mammary Gland Biol. Neoplasia 2008, 13:323-335.
    • (2008) J. Mammary Gland Biol. Neoplasia , vol.13 , pp. 323-335
    • Marcotte, R.1    Muller, W.J.2
  • 30
    • 34247474890 scopus 로고    scopus 로고
    • Tumour microenvironment: laminin 332 in squamous-cell carcinoma
    • Marinkovich M.P. Tumour microenvironment: laminin 332 in squamous-cell carcinoma. Nat. Rev. Cancer 2007, 7:370-380.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 370-380
    • Marinkovich, M.P.1
  • 31
  • 32
    • 80053061481 scopus 로고    scopus 로고
    • Beta1 integrin cytoplasmic tyrosines promote skin tumorigenesis independent of their phosphorylation
    • Meves A., Geiger T., Zanivan S., DiGiovanni J., Mann M., Fässler R. Beta1 integrin cytoplasmic tyrosines promote skin tumorigenesis independent of their phosphorylation. Proc. Natl. Acad. Sci. USA 2011, 108:15213-15218.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 15213-15218
    • Meves, A.1    Geiger, T.2    Zanivan, S.3    DiGiovanni, J.4    Mann, M.5    Fässler, R.6
  • 33
    • 75549084894 scopus 로고    scopus 로고
    • PANTHER version 7: improved phylogenetic trees, orthologs and collaboration with the Gene Ontology Consortium
    • Mi H., Dong Q., Muruganujan A., Gaudet P., Lewis S., Thomas P.D. PANTHER version 7: improved phylogenetic trees, orthologs and collaboration with the Gene Ontology Consortium. Nucleic Acids Res. 2010, 38(Database issue):D204-D210.
    • (2010) Nucleic Acids Res. , vol.38 , Issue.DATABASE ISSUE
    • Mi, H.1    Dong, Q.2    Muruganujan, A.3    Gaudet, P.4    Lewis, S.5    Thomas, P.D.6
  • 36
    • 79961014854 scopus 로고    scopus 로고
    • Large-scale phosphosite quantification in tissues by a spike-in SILAC method
    • Monetti M., Nagaraj N., Sharma K., Mann M. Large-scale phosphosite quantification in tissues by a spike-in SILAC method. Nat. Methods 2011, 8:655-658.
    • (2011) Nat. Methods , vol.8 , pp. 655-658
    • Monetti, M.1    Nagaraj, N.2    Sharma, K.3    Mann, M.4
  • 37
    • 10344250392 scopus 로고    scopus 로고
    • Retinoblastoma protein function and p16INK4a expression in actinic keratosis, squamous cell carcinoma in situ and invasive squamous cell carcinoma of the skin and links between p16INK4a expression and infiltrative behavior
    • Nilsson K., Svensson S., Landberg G. Retinoblastoma protein function and p16INK4a expression in actinic keratosis, squamous cell carcinoma in situ and invasive squamous cell carcinoma of the skin and links between p16INK4a expression and infiltrative behavior. Mod. Pathol. 2004, 17:1464-1474.
    • (2004) Mod. Pathol. , vol.17 , pp. 1464-1474
    • Nilsson, K.1    Svensson, S.2    Landberg, G.3
  • 38
    • 33748876374 scopus 로고    scopus 로고
    • Identification of differentially expressed genes in cutaneous squamous cell carcinoma by microarray expression profiling
    • Nindl I., Dang C., Forschner T., Kuban R.J., Meyer T., Sterry W., Stockfleth E. Identification of differentially expressed genes in cutaneous squamous cell carcinoma by microarray expression profiling. Mol. Cancer 2006, 5:30.
    • (2006) Mol. Cancer , vol.5 , pp. 30
    • Nindl, I.1    Dang, C.2    Forschner, T.3    Kuban, R.J.4    Meyer, T.5    Sterry, W.6    Stockfleth, E.7
  • 41
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127:635-648.
    • (2006) Cell , vol.127 , 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
  • 42
    • 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., Mann M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 2002, 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
  • 43
    • 77954378942 scopus 로고    scopus 로고
    • Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry
    • Ostasiewicz P., Zielinska D.F., Mann M., WiŚniewski J.R. Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry. J. Proteome Res. 2010, 9:3688-3700.
    • (2010) J. Proteome Res. , vol.9 , pp. 3688-3700
    • Ostasiewicz, P.1    Zielinska, D.F.2    Mann, M.3    WiŚniewski, J.R.4
  • 44
    • 20444383859 scopus 로고    scopus 로고
    • Protein phosphorylation in signaling-50 years and counting
    • Pawson T., Scott J.D. Protein phosphorylation in signaling-50 years and counting. Trends Biochem. Sci. 2005, 30:286-290.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 286-290
    • Pawson, T.1    Scott, J.D.2
  • 45
    • 0019960812 scopus 로고
    • A point mutation is responsible for the acquisition of transforming properties by the T24 human bladder carcinoma oncogene
    • Reddy E.P., Reynolds R.K., Santos E., Barbacid M. A point mutation is responsible for the acquisition of transforming properties by the T24 human bladder carcinoma oncogene. Nature 1982, 300:149-152.
    • (1982) Nature , vol.300 , pp. 149-152
    • Reddy, E.P.1    Reynolds, R.K.2    Santos, E.3    Barbacid, M.4
  • 46
    • 78650012935 scopus 로고    scopus 로고
    • Invasive three-dimensional organotypic neoplasia from multiple normal human epithelia
    • Ridky T.W., Chow J.M., Wong D.J., Khavari P.A. Invasive three-dimensional organotypic neoplasia from multiple normal human epithelia. Nat. Med. 2010, 16:1450-1455.
    • (2010) Nat. Med. , vol.16 , pp. 1450-1455
    • Ridky, T.W.1    Chow, J.M.2    Wong, D.J.3    Khavari, P.A.4
  • 49
    • 75149117479 scopus 로고    scopus 로고
    • Impact of feedback phosphorylation and Raf heterodimerization on normal and mutant B-Raf signaling
    • Ritt D.A., Monson D.M., Specht S.I., Morrison D.K. Impact of feedback phosphorylation and Raf heterodimerization on normal and mutant B-Raf signaling. Mol. Cell. Biol. 2010, 30:806-819.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 806-819
    • Ritt, D.A.1    Monson, D.M.2    Specht, S.I.3    Morrison, D.K.4
  • 51
    • 16444361960 scopus 로고    scopus 로고
    • Overexpression and hyperphosphorylation of retinoblastoma protein in the progression of malignant melanoma
    • Roesch A., Becker B., Meyer S., Hafner C., Wild P.J., Landthaler M., Vogt T. Overexpression and hyperphosphorylation of retinoblastoma protein in the progression of malignant melanoma. Mod. Pathol. 2005, 18:565-572.
    • (2005) Mod. Pathol. , vol.18 , pp. 565-572
    • Roesch, A.1    Becker, B.2    Meyer, S.3    Hafner, C.4    Wild, P.J.5    Landthaler, M.6    Vogt, T.7
  • 52
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz D., Gygi S.P. An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotechnol. 2005, 23:1391-1398.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 53
    • 78649880786 scopus 로고    scopus 로고
    • P21-activated kinase 4 regulates ovarian cancer cell proliferation, migration, and invasion and contributes to poor prognosis in patients
    • Siu M.K., Chan H.Y., Kong D.S., Wong E.S., Wong O.G., Ngan H.Y., Tam K.F., Zhang H., Li Z., Chan Q.K., et al. p21-activated kinase 4 regulates ovarian cancer cell proliferation, migration, and invasion and contributes to poor prognosis in patients. Proc. Natl. Acad. Sci. USA 2010, 107:18622-18627.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18622-18627
    • Siu, M.K.1    Chan, H.Y.2    Kong, D.S.3    Wong, E.S.4    Wong, O.G.5    Ngan, H.Y.6    Tam, K.F.7    Zhang, H.8    Li, Z.9    Chan, Q.K.10
  • 57
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • Tusher V.G., Tibshirani R., Chu G. Significance analysis of microarrays applied to the ionizing radiation response. Proc. Natl. Acad. Sci. USA 2001, 98:5116-5121.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3
  • 60
    • 47049127002 scopus 로고    scopus 로고
    • Regulation of proline-rich Akt substrate of 40 kDa (PRAS40) function by mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation
    • Wang L., Harris T.E., Lawrence J.C. Regulation of proline-rich Akt substrate of 40 kDa (PRAS40) function by mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation. J. Biol. Chem. 2008, 283:15619-15627.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15619-15627
    • Wang, L.1    Harris, T.E.2    Lawrence, J.C.3
  • 61
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski J.R., Zougman A., Nagaraj N., Mann M. Universal sample preparation method for proteome analysis. Nat. Methods 2009, 6:359-362.
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 62
    • 50449087307 scopus 로고    scopus 로고
    • Loss of desmoglein 1 expression associated with worse prognosis in head and neck squamous cell carcinoma patients
    • Wong M.P., Cheang M., Yorida E., Coldman A., Gilks C.B., Huntsman D., Berean K. Loss of desmoglein 1 expression associated with worse prognosis in head and neck squamous cell carcinoma patients. Pathology 2008, 40:611-616.
    • (2008) Pathology , vol.40 , pp. 611-616
    • Wong, M.P.1    Cheang, M.2    Yorida, E.3    Coldman, A.4    Gilks, C.B.5    Huntsman, D.6    Berean, K.7
  • 63
    • 78650552589 scopus 로고    scopus 로고
    • Forcing form and function: biomechanical regulation of tumor evolution
    • Yu H., Mouw J.K., Weaver V.M. Forcing form and function: biomechanical regulation of tumor evolution. Trends Cell Biol. 2011, 21:47-56.
    • (2011) Trends Cell Biol. , vol.21 , pp. 47-56
    • Yu, H.1    Mouw, J.K.2    Weaver, V.M.3
  • 64
    • 77951737987 scopus 로고    scopus 로고
    • The switchable integrin adhesome
    • Zaidel-Bar R., Geiger B. The switchable integrin adhesome. J. Cell Sci. 2010, 123:1385-1388.
    • (2010) J. Cell Sci. , vol.123 , pp. 1385-1388
    • Zaidel-Bar, R.1    Geiger, B.2
  • 66
    • 80054723147 scopus 로고    scopus 로고
    • In vivo quantitative proteomics: the SILAC mouse
    • Zanivan S., Krueger M., Mann M. In vivo quantitative proteomics: the SILAC mouse. Methods Mol. Biol. 2012, 757:435-450.
    • (2012) Methods Mol. Biol. , vol.757 , pp. 435-450
    • Zanivan, S.1    Krueger, M.2    Mann, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.