메뉴 건너뛰기




Volumn 8, Issue 374, 2015, Pages

Dynamic phosphoproteomics reveals TORC1-dependent regulation of yeast nucleotide and amino acid biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

AMD1; ATG1; FUNGAL ENZYME; FUNGAL PROTEIN; HOM3; NITROGEN; PHOSPHATASE; PHOSPHOTRANSFERASE; RAPAMYCIN; SCH9; TARGET OF RAPAMYCIN COMPLEX 1; TRANSCRIPTION FACTOR; TSL1; UNCLASSIFIED DRUG; AMINO ACID; NUCLEOTIDE; PHOSPHOPROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; TORC1 PROTEIN COMPLEX, S CEREVISIAE;

EID: 84928723640     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2005768     Document Type: Article
Times cited : (62)

References (57)
  • 8
    • 69249240179 scopus 로고    scopus 로고
    • Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis
    • A. Huber, B. Bodenmiller, A. Uotila, M. Stahl, S.Wanka, B. Gerrits, R. Aebersold, R. Loewith, Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis. Genes Dev. 23, 1929-1943 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 1929-1943
    • Huber, A.1    Bodenmiller, B.2    Uotila, A.3    Stahl, M.4    Wanka, S.5    Gerrits, B.6    Aebersold, R.7    Loewith, R.8
  • 9
    • 77958031723 scopus 로고    scopus 로고
    • The rapamycinsensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates
    • A. Soulard, A. Cremonesi, S. Moes, F. Schütz, P. Jenö, M. N. Hall, The rapamycinsensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates. Mol. Biol. Cell 21, 3475-3486 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3475-3486
    • Soulard, A.1    Cremonesi, A.2    Moes, S.3    Schütz, F.4    Jenö, P.5    Hall, M.N.6
  • 13
    • 70349131530 scopus 로고    scopus 로고
    • The phosphoproteomics data explosion
    • S. Lemeer, A. J. Heck, The phosphoproteomics data explosion. Curr. Opin. Chem. Biol. 13, 414-420 (2009).
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 414-420
    • Lemeer, S.1    Heck, A.J.2
  • 16
  • 17
    • 65349155149 scopus 로고    scopus 로고
    • Weak functional constraints on phosphoproteomes
    • C. R. Landry, E. D. Levy, S. W. Michnick, Weak functional constraints on phosphoproteomes. Trends Genet. 25, 193-197 (2009).
    • (2009) Trends Genet. , vol.25 , pp. 193-197
    • Landry, C.R.1    Levy, E.D.2    Michnick, S.W.3
  • 18
    • 48149087568 scopus 로고    scopus 로고
    • Non-functional phosphorylations?
    • G. E. Lienhard, Non-functional phosphorylations? Trends Biochem. Sci. 33, 351-352 (2008).
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 351-352
    • Lienhard, G.E.1
  • 20
    • 84878628963 scopus 로고    scopus 로고
    • Phosphoproteome dynamics reveal novel ERK1/2 MAP kinase substrates with broad spectrum of functions
    • M. Courcelles, C. Frémin, L. Voisin, S. Lemieux, S. Meloche, P. Thibault, Phosphoproteome dynamics reveal novel ERK1/2 MAP kinase substrates with broad spectrum of functions. Mol. Syst. Biol. 9, 669 (2013).
    • (2013) Mol. Syst. Biol. , vol.9 , pp. 669
    • Courcelles, M.1    Frémin, C.2    Voisin, L.3    Lemieux, S.4    Meloche, S.5    Thibault, P.6
  • 23
    • 83455177213 scopus 로고    scopus 로고
    • Target of rapamycin (TOR) in nutrient signaling and growth control
    • R. Loewith, M. N. Hall, Target of rapamycin (TOR) in nutrient signaling and growth control. Genetics 189, 1177-1201 (2011).
    • (2011) Genetics , vol.189 , pp. 1177-1201
    • Loewith, R.1    Hall, M.N.2
  • 25
    • 79953207023 scopus 로고    scopus 로고
    • A brief history of TOR
    • R. Loewith, A brief history of TOR. Biochem. Soc. Trans. 39, 437-442 (2011).
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 437-442
    • Loewith, R.1
  • 28
    • 0033592983 scopus 로고    scopus 로고
    • Rapamycin-modulated transcription defines the subset of nutrient-sensitive signaling pathways directly controlled by the Tor proteins
    • J. S. Hardwick, F. G. Kuruvilla, J. K. Tong, A. F. Shamji, S. L. Schreiber, Rapamycin-modulated transcription defines the subset of nutrient-sensitive signaling pathways directly controlled by the Tor proteins. Proc. Natl. Acad. Sci. U.S.A. 96, 14866-14870 (1999).
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14866-14870
    • Hardwick, J.S.1    Kuruvilla, F.G.2    Tong, J.K.3    Shamji, A.F.4    Schreiber, S.L.5
  • 30
    • 84874995247 scopus 로고    scopus 로고
    • Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1
    • I. Ben-Sahra, J. J. Howell, J. M. Asara, B. D. Manning, Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1. Science 339, 1323-1328 (2013).
    • (2013) Science , vol.339 , pp. 1323-1328
    • Ben-Sahra, I.1    Howell, J.J.2    Asara, J.M.3    Manning, B.D.4
  • 32
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • J. K. Eng, A. L. McCormack, J. R. Yates, An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989 (1994).
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 33
    • 84887052462 scopus 로고    scopus 로고
    • LuciPHOr: Algorithm for phosphorylation site localization with false localization rate estimation using modified target-decoy approach
    • D. Fermin, S. J. Walmsley, A. C. Gingras, H. Choi, A. I. Nesvizhskii, LuciPHOr: Algorithm for phosphorylation site localization with false localization rate estimation using modified target-decoy approach. Mol. Cell. Proteomics 12, 3409-3419 (2013).
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3409-3419
    • Fermin, D.1    Walmsley, S.J.2    Gingras, A.C.3    Choi, H.4    Nesvizhskii, A.I.5
  • 35
    • 33751191872 scopus 로고    scopus 로고
    • Nitrogen availability and TOR regulate the Snf1 protein kinase in Saccharomyces cerevisiae
    • M. Orlova, E. Kanter, D. Krakovich, S. Kuchin, Nitrogen availability and TOR regulate the Snf1 protein kinase in Saccharomyces cerevisiae. Eukaryot. Cell 5, 1831-1837 (2006).
    • (2006) Eukaryot. Cell , vol.5 , pp. 1831-1837
    • Orlova, M.1    Kanter, E.2    Krakovich, D.3    Kuchin, S.4
  • 36
    • 60149091050 scopus 로고    scopus 로고
    • Identification of the rapamycin-sensitive phosphorylation sites within the Ser/Thr-rich domain of the yeast Npr1 protein kinase
    • S. Gander, D. Bonenfant, P. Altermatt, D. E. Martin, S. Hauri, S. Moes, M. N. Hall, P. Jenoe, Identification of the rapamycin-sensitive phosphorylation sites within the Ser/Thr-rich domain of the yeast Npr1 protein kinase. Rapid Commun. Mass Spectrom. 22, 3743-3753 (2008).
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 3743-3753
    • Gander, S.1    Bonenfant, D.2    Altermatt, P.3    Martin, D.E.4    Hauri, S.5    Moes, S.6    Hall, M.N.7    Jenoe, P.8
  • 38
    • 84873190824 scopus 로고    scopus 로고
    • Yeast endosulfines control entry into quiescence and chronological life span by inhibiting protein phosphatase 2A
    • S. Bontron, M. Jaquenoud, S. Vaga, N. Talarek, B. Bodenmiller, R. Aebersold, C. De Virgilio, Yeast endosulfines control entry into quiescence and chronological life span by inhibiting protein phosphatase 2A. Cell Rep. 3, 16-22 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 16-22
    • Bontron, S.1    Jaquenoud, M.2    Vaga, S.3    Talarek, N.4    Bodenmiller, B.5    Aebersold, R.6    De Virgilio, C.7
  • 40
    • 77954523086 scopus 로고    scopus 로고
    • Options and considerations when selecting a quantitative proteomics strategy
    • B. Domon, R. Aebersold, Options and considerations when selecting a quantitative proteomics strategy. Nat. Biotechnol. 28, 710-721 (2010).
    • (2010) Nat. Biotechnol. , vol.28 , pp. 710-721
    • Domon, B.1    Aebersold, R.2
  • 42
    • 66249102308 scopus 로고    scopus 로고
    • Multisite protein phosphorylation-From molecular mechanisms to kinetic models
    • C. Salazar, T. Höfer, Multisite protein phosphorylation-From molecular mechanisms to kinetic models. FEBS J. 276, 3177-3198 (2009).
    • (2009) FEBS J. , vol.276 , pp. 3177-3198
    • Salazar, C.1    Höfer, T.2
  • 45
    • 41049102359 scopus 로고    scopus 로고
    • Architecture of transcriptional regulatory circuits is knitted over the topology of bio-molecular interaction networks
    • A. P. Oliveira, K. R. Patil, J. Nielsen, Architecture of transcriptional regulatory circuits is knitted over the topology of bio-molecular interaction networks. BMC Syst. Biol. 2, 17 (2008).
    • (2008) BMC Syst. Biol. , vol.2 , pp. 17
    • Oliveira, A.P.1    Patil, K.R.2    Nielsen, J.3
  • 46
    • 14544268137 scopus 로고    scopus 로고
    • Uncovering transcriptional regulation of metabolism by using metabolic network topology
    • K. R. Patil, J. Nielsen, Uncovering transcriptional regulation of metabolism by using metabolic network topology. Proc. Natl. Acad. Sci. U.S.A. 102, 2685-2689 (2005).
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 2685-2689
    • Patil, K.R.1    Nielsen, J.2
  • 47
    • 84884544927 scopus 로고    scopus 로고
    • Five conditions commonly used to down-regulate tor complex 1 generate different physiological situations exhibiting distinct requirements and outcomes
    • J. J. Tate, T. G. Cooper, Five conditions commonly used to down-regulate tor complex 1 generate different physiological situations exhibiting distinct requirements and outcomes. J. Biol. Chem. 288, 27243-27262 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 27243-27262
    • Tate, J.J.1    Cooper, T.G.2
  • 48
    • 78649704325 scopus 로고    scopus 로고
    • Autophagy and metabolism
    • J. D. Rabinowitz, E. White, Autophagy and metabolism. Science 330, 1344-1348 (2010).
    • (2010) Science , vol.330 , pp. 1344-1348
    • Rabinowitz, J.D.1    White, E.2
  • 50
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • B. Bodenmiller, L. N. Mueller, M. Mueller, B. Domon, R. Aebersold, Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat. Methods 4, 231-237 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 52
    • 0002432565 scopus 로고
    • Multivariate adaptive regression splines
    • J. H. Friedman, Multivariate adaptive regression splines. Ann. Stat. 19, 1-141 (1991).
    • (1991) Ann. Stat. , vol.19 , pp. 1-141
    • Friedman, J.H.1
  • 54
    • 84857518627 scopus 로고    scopus 로고
    • Biological sequence motif discovery using motif-x
    • Chapter 13, Unit 13.15-24
    • M. F. Chou, D. Schwartz, Biological sequence motif discovery using motif-x. Curr. Protoc. Bioinformatics Chapter 13, Unit 13.15-24 (2011).
    • (2011) Curr. Protoc. Bioinformatics
    • Chou, M.F.1    Schwartz, D.2
  • 55
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • D. Schwartz, S. P. Gygi, An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotechnol. 23, 1391-1398 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 56
    • 33847172327 scopus 로고    scopus 로고
    • Clustering by passing messages between data points
    • B. J. Frey, D. Dueck, Clustering by passing messages between data points. Science 315, 972-976 (2007).
    • (2007) Science , vol.315 , pp. 972-976
    • Frey, B.J.1    Dueck, D.2
  • 57
    • 65649126379 scopus 로고    scopus 로고
    • Connecting extracellular metabolomic measurements to intracellular flux states in yeast
    • M. L. Mo, B. O. Palsson, M. J. Herrgård, Connecting extracellular metabolomic measurements to intracellular flux states in yeast. BMC Syst. Biol. 3, 37 (2009).
    • (2009) BMC Syst. Biol. , vol.3 , pp. 37
    • Mo, M.L.1    Palsson, B.O.2    Herrgård, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.