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Mol Syst Biol

Title:		Phosphoproteomic analyses reveal novel cross-modulation mechanisms between two signaling pathways in yeast
Author(s):		Vaga S; Bernardo-Faura M; Cokelaer T; Maiolica A; Barnes CA; Gillet LC; Hegemann B; van Drogen F; Sharifian H; Klipp E; Peter M; Saez-Rodriguez J; Aebersold R;
Address:		"Department of Biology, Institute of Molecular Systems Biology ETH Zurich, Zurich, Switzerland. European Molecular Biology Laboratory (EMBL), European Bioinformatics Institute (EBI), Cambridge, UK. Department of Biology, Institute of Molecular Systems Biology ETH Zurich, Zurich, Switzerland Department of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland. Department of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland. Department of Biology, Theoretical Biophysics, Humboldt-Universitat zu Berlin, Berlin, Germany. Department of Biology, Institute of Molecular Systems Biology ETH Zurich, Zurich, Switzerland Faculty of Science, University of Zurich, Zurich, Switzerland aebersold@imsb.biol.ethz.ch"
Journal Title:		Mol Syst Biol
Year:		2014
Volume:		20141209
Issue:		12
Page Number:		767 -
DOI:		10.15252/msb.20145112
ISSN/ISBN:		1744-4292 (Electronic) 1744-4292 (Print) 1744-4292 (Linking)
Abstract:		"Cells respond to environmental stimuli via specialized signaling pathways. Concurrent stimuli trigger multiple pathways that integrate information, predominantly via protein phosphorylation. Budding yeast responds to NaCl and pheromone via two mitogen-activated protein kinase cascades, the high osmolarity, and the mating pathways, respectively. To investigate signal integration between these pathways, we quantified the time-resolved phosphorylation site dynamics after pathway co-stimulation. Using shotgun mass spectrometry, we quantified 2,536 phosphopeptides across 36 conditions. Our data indicate that NaCl and pheromone affect phosphorylation events within both pathways, which thus affect each other at more levels than anticipated, allowing for information exchange and signal integration. We observed a pheromone-induced down-regulation of Hog1 phosphorylation due to Gpd1, Ste20, Ptp2, Pbs2, and Ptc1. Distinct Ste20 and Pbs2 phosphosites responded differently to the two stimuli, suggesting these proteins as key mediators of the information exchange. A set of logic models was then used to assess the role of measured phosphopeptides in the crosstalk. Our results show that the integration of the response to different stimuli requires complex interconnections between signaling pathways"
Keywords:		"Down-Regulation Mitogen-Activated Protein Kinases/genetics/metabolism Models, Theoretical Osmolar Concentration Pheromones/*metabolism Phosphorylation Proteome/*metabolism Saccharomyces cerevisiae/*genetics Saccharomyces cerevisiae Proteins/genetics/metab;"
Notes:		"MedlineVaga, Stefania Bernardo-Faura, Marti Cokelaer, Thomas Maiolica, Alessio Barnes, Christopher A Gillet, Ludovic C Hegemann, Bjorn van Drogen, Frank Sharifian, Hoda Klipp, Edda Peter, Matthias Saez-Rodriguez, Julio Aebersold, Ruedi eng Research Support, Non-U.S. Gov't England 2014/12/11 Mol Syst Biol. 2014 Dec 9; 10(12):767. doi: 10.15252/msb.20145112"