ArticleMolecular systems biology2014
Phosphoproteomic analyses reveal novel cross-modulation mechanisms between two signaling pathways in yeast.
Article in Molecular systems biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 56 citations in OpenAlex.
- Harnessing the PpHog1 Regulatory Network to Engineer a UPR-Adaptive Komagataella phaffii Chassis for High-Copy Secretory Protein Production.Microbial biotechnology · 2026Article
- Lysosome-dependent nutrient scavenging underlies stress adaptation during epithelial-to-mesenchymal transition.bioRxiv : the preprint server for biology · 2025Article
- Systems-level reconstruction of kinase phosphosignaling networks regulating endothelial barrier integrity using temporal data.NPJ systems biology and applications · 2024Article
- Systems-level reconstruction of kinase phosphosignaling networks regulating endothelial barrier integrity using temporal data.bioRxiv : the preprint server for biology · 2024Article
- Interrogating endothelial barrier regulation by temporally resolved kinase network generation.Life science alliance · 2024Article
- The regulatory landscape of the yeast phosphoproteome.Nature structural & molecular biology · 2023Article
- Reducing Boolean networks with backward equivalence.BMC bioinformatics · 2023Article
- Positive feedback induces switch between distributive and processive phosphorylation of Hog1.Nature communications · 2023Article
- Pharmacological approaches to understanding protein kinase signaling networks.Frontiers in pharmacology · 2023Review
- Ultrastructural plasma membrane asymmetries in tension and curvature promote yeast cell fusion.The Journal of cell biology · 2021Article
- Dynamic Transcriptomic and Phosphoproteomic Analysis During Cell Wall Stress inMolecular & cellular proteomics : MCP · 2020Article
- Crosstalk and spatiotemporal regulation between stress-induced MAP kinase pathways and pheromone signaling in budding yeast.Cell cycle (Georgetown, Tex.) · 2020Review
- R2-P2 rapid-robotic phosphoproteomics enables multidimensional cell signaling studies.Molecular systems biology · 2019Article
- Mechanical stress impairs pheromone signaling via Pkc1-mediated regulation of the MAPK scaffold Ste5.The Journal of cell biology · 2019Article
- Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages.Cell communication and signaling : CCS · 2019Article
- Article
- Reconstructing phosphorylation signalling networks from quantitative phosphoproteomic data.Essays in biochemistry · 2018Review
- REFINING CELLULAR PATHWAY MODELS USING AN ENSEMBLE OF HETEROGENEOUS DATA SOURCES.The annals of applied statistics · 2018Article
- SimPhospho: a software tool enabling confident phosphosite assignment.Bioinformatics (Oxford, England) · 2018Article
- Identifying protein kinase-specific effectors of the osmostress response in yeast.Science signaling · 2017Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.