ArticleMolecular & cellular proteomics : MCP2013
Phosphoproteomic analysis of protein kinase C signaling in Saccharomyces cerevisiae reveals Slt2 mitogen-activated protein kinase (MAPK)-dependent phosphorylation of eisosome core components.
Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 63 citations in OpenAlex.
- The transcription factor Rlm1 couples the MAPK Slt2/ERK1 pathway to the IRE1-driven unfolded protein response.Communications biology · 2026Article
- Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response.Nature communications · 2025Article
- Coupling the MAPK Slt2/ERK1 Pathway and IRE1-driven UPR Through Transcription Factor Rlm1/MEF2.Research square · 2025Article
- The protein phosphatase 2C domain contributes to the pathobiological function of adenylyl cyclase inbioRxiv : the preprint server for biology · 2025Article
- Bni5 regulates and coordinates septin architecture and myosin-II functions at the cell division site.The Journal of cell biology · 2025Article
- The small GTPase Rho5-Yet another player in yeast glucose signaling.PLoS genetics · 2025Article
- Activation of the cell wall integrity pathway negatively regulates TORC2-Ypk1/2 signaling through blocking eisosome disassembly in Saccharomyces cerevisiae.Communications biology · 2024Article
- Aspergillus fumigatus mitogen-activated protein kinase MpkA is involved in gliotoxin production and self-protection.Nature communications · 2024Article
- Inducible degradation-coupled phosphoproteomics identifies PP2AFrontiers in cell and developmental biology · 2024Article
- A Multimodel Study of the Role of Novel PKC Isoforms in the DNA Integrity Checkpoint.International journal of molecular sciences · 2023Article
- The phosphatase Glc7 controls the eisosomal response to starvation via post-translational modification of Pil1.Journal of cell science · 2023Article
- SILAC-Based Quantitative Phosphoproteomics in Yeast.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Substrates of the MAPK Slt2: Shaping Yeast Cell Integrity.Journal of fungi (Basel, Switzerland) · 2022Review
- The Fission Yeast Cell Integrity Pathway: A Functional Hub for Cell Survival upon Stress and Beyond.Journal of fungi (Basel, Switzerland) · 2021Review
- The CWI Pathway: A Versatile Toolbox to Arrest Cell-Cycle Progression.Journal of fungi (Basel, Switzerland) · 2021Review
- A walk-through MAPK structure and functionality with the 30-year-old yeast MAPK Slt2.International microbiology : the official journal of the Spanish Society for Microbiology · 2021Review
- The Role of the Cell Integrity Pathway in Septum Assembly in Yeast.Journal of fungi (Basel, Switzerland) · 2021Review
- Effect of Static Magnetic Field onJournal of fungi (Basel, Switzerland) · 2021Article
- Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020Review
- Physiological responses of Saccharomyces cerevisiae to industrially relevant conditions: Slow growth, low pH, and high COBiotechnology and bioengineering · 2020Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell wall integrity (CWI) pathway of the model organism Saccharomyces cerevisiae has been thoroughly studied as a paradigm of the mitogen-activated protein kinase (MAPK) pathway. It consists of a classic MAPK module comprising the Bck1 MAPK kinase kinase, two redundant MAPK kinases (Mkk1 and Mkk2), and the Slt2 MAPK. This module is activated under a variety of stimuli related to cell wall homeostasis by Pkc1, the only member of the protein kinase C family in budding yeast. Quantitative phosphoproteomics based on stable isotope labeling of amino acids in cell culture is a powerful tool for globally studying protein phosphorylation. Here we report an analysis of the yeast phosphoproteome upon overexpression of a PKC1 hyperactive allele that specifically activates CWI MAPK signaling in the absence of external stimuli. We found 82 phosphopeptides originating from 43 proteins that showed enhanced phosphorylation in these conditions. The MAPK S/T-P target motif was significantly overrepresented in these phosphopeptides. Hyperphosphorylated proteins provide putative novel targets of the Pkc1-cell wall integrity pathway involved in diverse functions such as the control of gene expression, protein synthesis, cytoskeleton maintenance, DNA repair, and metabolism. Remarkably, five components of the plasma-membrane-associated protein complex known as eisosomes were found among the up-regulated proteins. We show here that Pkc1-induced phosphorylation of the eisosome core components Pil1 and Lsp1 was not exerted directly by Pkc1, but involved signaling through the Slt2 MAPK module.
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