Phosphoproteomic analysis reveals interconnected system-wide responses to perturbations of kinases and phosphatases in yeast

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The phosphorylation and dephosphorylation of proteins by kinases and phosphatases constitute an essential regulatory network in eukaryotic cells. This network supports the flow of information from sensors through signaling systems to effector molecules, and ultimately drives the phenotype and functi...

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Autor principal: Bodenmiller, B.
Otros Autores: Wanka, S., Kraft, C., Urban, J., Campbell, D., Pedrioli, P.G, Gerrits, B., Picotti, P., Lam, H., Vitek, O., Brusniak, M.-Y, Roschitzki, B., Zhang, C., Shokat, K.M, Schlapbach, R., Colman-Lerner, A., Nolan, G.P, Nesvizhskii, A.I, Peter, M., Loewith, R., Mering, C.V, Aebersold, R.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2010
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 cas  |a phosphatase, 9013-05-2; protein kinase, 9026-43-1; phosphotransferase, 9031-09-8, 9031-44-1; Phosphoproteins; Phosphoric Monoester Hydrolases, 3.1.3.-; Phosphotransferases, 2.7.- 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
100 1 |a Bodenmiller, B. 
245 1 0 |a Phosphoproteomic analysis reveals interconnected system-wide responses to perturbations of kinases and phosphatases in yeast 
260 |c 2010 
270 1 0 |m Aebersold, R.; Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, Switzerland; email: aebersold@imsb.biol.ethz.ch 
506 |2 openaire  |e Política editorial 
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504 |a Acknowledgments: We thank the whole team of the Functional Genomics Center Zurich (FGCZ) for fruitful discussions. We thank C. Zheng, Department of Statistics, Purdue University, for help with use and interpretation of the Limma package. Funding: This project was funded in part by ETH Zurich; Federal funds from the National Heart, Lung, and Blood Institute, NIH, under contract no. N01-HV-28179; the PhosphoNetX project of SystemsX.ch, the Swiss initiative for systems biology; and the European Research Council (grant ERC-2008-AdG 233226) to R.A. Work at the FGCZ and at the von Mering laboratory has been supported by the University Research Priority Program Systems Biology and Functional Genomics of the University of Zurich. B.G. is supported by the Bonizzi-Theler Foundation. C.K. is supported by a Marie-Heim Vögtlin fellowship from the Swiss National Science Foundation (SNF) 
520 3 |a The phosphorylation and dephosphorylation of proteins by kinases and phosphatases constitute an essential regulatory network in eukaryotic cells. This network supports the flow of information from sensors through signaling systems to effector molecules, and ultimately drives the phenotype and function of cells, tissues, and organisms. Dysregulation of this process has severe consequencesand is one of the main factors in the emergence and progression of diseases, including cancer. Thus, major efforts have been invested in developing specific inhibitors that modulate the activity of individual kinases or phosphatases; however, it has been difficult to assess how such pharmacological interventions would affect the cellular signaling network as a whole. Here, we used label-free, quantitative phosphoproteomics in a systematically perturbed model organism (Saccharomyces cerevisiae) to determine the relationships between 97 kinases, 27 phosphatases, and more than 1000 phosphoproteins. We identified 8814 regulated phosphorylation events, describing the first system-wide protein phosphorylation network in vivo. Our results show that, at steady state, inactivation of most kinases and phosphatases affected large parts of the phosphorylation-modulated signal transduction machinery, and not only the immediate downstream targets. The observed cellular growth phenotype was often well maintained despite the perturbations, arguing for considerable robustness in the system. Our results serve to constrain future models of cellular signaling and reinforce the idea that simple linear representations of signaling pathways might be insufficient for drug development and for describing organismal homeostasis. © 2008 American Association for the Advancement of Science.  |l eng 
593 |a Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, Switzerland 
593 |a Zurich PhD Program in Molecular Life Sciences, 8057 Zurich, Switzerland 
593 |a Institute of Molecular Life Sciences, Swiss Institute of Bioinformatics, University of Zurich, 8057 Zurich, Switzerland 
593 |a Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland 
593 |a Department of Molecular Biology, University of Geneva, Geneva 1211, Switzerland 
593 |a Institute for Systems Biology, Seattle, WA 98103, United States 
593 |a Functional Genomics Center Zurich, University Zurich and ETH Zurich, 8057 Zurich, Switzerland 
593 |a Department of Chemical and Biomolecular Engineering, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, Hong Kong 
593 |a Departments of Statistics and Computer Science, Purdue University, West Lafayette, IN 47107, United States 
593 |a Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158-2280, United States 
593 |a Facultad de Ciencias Exactasy Naturales, University of Buenos Aires, C1428EHA Buenos Aires, Argentina 
593 |a Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, United States 
593 |a Department of Pathology, University of Michigan, Ann Arbor, MI 48109, United States 
593 |a Faculty of Science, University of Zurich, 8057 Zurich, Switzerland 
593 |a Scottish Institute for Cell Signalling, Sir James Black Centre, University of Dundee, Dundee, DD1 5EH, United Kingdom 
593 |a Novartis Institute for Biomedical Research, Novartis International, AG, CH-4002 Basel, Switzerland 
690 1 0 |a PHOSPHATASE 
690 1 0 |a PHOSPHOPROTEIN 
690 1 0 |a PROTEIN KINASE 
690 1 0 |a PHOSPHATASE 
690 1 0 |a PHOSPHOPROTEIN 
690 1 0 |a PHOSPHOTRANSFERASE 
690 1 0 |a ARTICLE 
690 1 0 |a CELL GROWTH 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a ENZYME ACTIVATION 
690 1 0 |a HEMOSTASIS 
690 1 0 |a IN VIVO STUDY 
690 1 0 |a NONHUMAN 
690 1 0 |a PHENOTYPE 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN ANALYSIS 
690 1 0 |a PROTEIN PHOSPHORYLATION 
690 1 0 |a PROTEOMICS 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a BAYES THEOREM 
690 1 0 |a BIOLOGICAL MODEL 
690 1 0 |a COMPARATIVE STUDY 
690 1 0 |a GENE DELETION 
690 1 0 |a GENETICS 
690 1 0 |a LIQUID CHROMATOGRAPHY 
690 1 0 |a METABOLISM 
690 1 0 |a METHODOLOGY 
690 1 0 |a PHOSPHORYLATION 
690 1 0 |a PHYSIOLOGY 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a SPECIES DIFFERENCE 
690 1 0 |a TANDEM MASS SPECTROMETRY 
690 1 0 |a EUKARYOTA 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
690 1 0 |a BAYES THEOREM 
690 1 0 |a CHROMATOGRAPHY, LIQUID 
690 1 0 |a GENE DELETION 
690 1 0 |a METABOLIC NETWORKS AND PATHWAYS 
690 1 0 |a MODELS, BIOLOGICAL 
690 1 0 |a PHOSPHOPROTEINS 
690 1 0 |a PHOSPHORIC MONOESTER HYDROLASES 
690 1 0 |a PHOSPHORYLATION 
690 1 0 |a PHOSPHOTRANSFERASES 
690 1 0 |a PROTEOMICS 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a SPECIES SPECIFICITY 
690 1 0 |a TANDEM MASS SPECTROMETRY 
700 1 |a Wanka, S. 
700 1 |a Kraft, C. 
700 1 |a Urban, J. 
700 1 |a Campbell, D. 
700 1 |a Pedrioli, P.G. 
700 1 |a Gerrits, B. 
700 1 |a Picotti, P. 
700 1 |a Lam, H. 
700 1 |a Vitek, O. 
700 1 |a Brusniak, M.-Y. 
700 1 |a Roschitzki, B. 
700 1 |a Zhang, C. 
700 1 |a Shokat, K.M. 
700 1 |a Schlapbach, R. 
700 1 |a Colman-Lerner, A. 
700 1 |a Nolan, G.P. 
700 1 |a Nesvizhskii, A.I. 
700 1 |a Peter, M. 
700 1 |a Loewith, R. 
700 1 |a Mering, C.V. 
700 1 |a Aebersold, R. 
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856 4 0 |u https://doi.org/10.1126/scisignal.2001182  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_19450877_v3_n153_p_Bodenmiller  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19450877_v3_n153_p_Bodenmiller  |y Registro en la Biblioteca Digital 
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