ArticleMolecular & cellular proteomics : MCP2014
Phosphoproteomic analysis of protein phosphorylation networks in Tetrahymena thermophila, a model single-celled organism.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 32 citations in OpenAlex.
- Integrative Proteomic Analysis Implicates Inhibition of Intracellular Protein Trafficking in Therapy-Induced Migrastasis in Prostate Cancer.Proteomes · 2026Article
- Comparative analysis of phosphorylated proteomes between plerocercoid and adult Spirometra mansoni reveals phosphoproteomic profiles of the medical tapeworm.Parasites & vectors · 2024Article
- Quantitative phosphoproteomics reveals molecular pathway network in wheat resistance to stripe rust.Stress biology · 2024Article
- A practical reference for studying meiosis in the model ciliateMarine life science & technology · 2022Review
- Transcriptomic Differences between Free-Living and ParasiticMicroorganisms · 2022Article
- Protein phosphorylation networks in spargana of Spirometra erinaceieuropaei revealed by phosphoproteomic analysis.Parasites & vectors · 2020Article
- Evolution of protein kinase substrate recognition at the active site.PLoS biology · 2019Article
- Functional Proteomics of Nuclear Proteins inGenes · 2019Review
- Phosphorylation of an HP1-like protein is a prerequisite for heterochromatin body formation in Tetrahymena DNA elimination.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Phosphorylation of an HP1-like Protein Regulates Heterochromatin Body Assembly for DNA Elimination.Developmental cell · 2015Article
- Crosstalk analysis of pathways in breast cancer using a network model based on overlapping differentially expressed genes.Experimental and therapeutic medicine · 2015Article
- Analysis of the Candida albicans Phosphoproteome.Eukaryotic cell · 2015Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tetrahymena thermophila is a widely used unicellular eukaryotic model organism in biological research and contains more than 1000 protein kinases and phosphatases with specificity for Ser/Thr/Tyr residues. However, only a few dozen phosphorylation sites in T. thermophila are known, presenting a major obstacle to further understanding of the regulatory roles of reversible phosphorylation in this organism. In this study, we used high-accuracy mass-spectrometry-based proteomics to conduct global and site-specific phosphoproteome profiling of T. thermophila. In total, 1384 phosphopeptides and 2238 phosphorylation sites from 1008 T. thermophila proteins were identified through the combined use of peptide prefractionation, TiO2 enrichment, and two-dimensional LC-MS/MS analysis. The identified phosphoproteins are implicated in the regulation of various biological processes such as transport, gene expression, and mRNA metabolic process. Moreover, integrated analysis of the T. thermophila phosphoproteome and gene network revealed the potential biological functions of many previously unannotated proteins and predicted some putative kinase-substrate pairs. Our data provide the first global survey of phosphorylation in T. thermophila using a phosphoproteomic approach and suggest a wide-ranging regulatory scope of this modification. The provided dataset is a valuable resource for the future understanding of signaling pathways in this important model organism.
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