ArticleScience signaling2010
Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs.
Article in Science signaling, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 226 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
226 citing papers in PubMed, 366 citations in OpenAlex.
- Crosstalk between protein kinases Pho85-Pho80 and Rim11 regulates Pah1 phosphatidate phosphatase function in lipid synthesis.The Journal of biological chemistry · 2026Article
- A deep learning and large language hybrid workflow for omics interpretation.Nature biomedical engineering · 2026Article
- An AI-enabled structural atlas decodes kinase specificity across the human proteome.Nature biotechnology · 2026Article
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- Protocol to study direct (de)phosphorylation events on a proteome-wide scale using on-bead in vitro enzyme assays.STAR protocols · 2026Article
- Decoding Cdk1 control: from mitotic thresholds to meiotic specificity.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026Review
- Structural bases of signal generation and transduction by the SPS amino acid sensor of Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- Article
- The fast-evolving FIKK kinase family of Plasmodium falciparum can be inhibited by a single compound.Nature microbiology · 2025Article
- The Yeast Gsk-3 Kinase Mck1 Is Necessary for Cell Wall Remodeling in Glucose-Starved and Cell Wall-Stressed Cells.International journal of molecular sciences · 2025Article
- Article
- Mck1-mediated proteolysis of CENP-A prevents mislocalization of CENP-A for chromosomal stability in Saccharomyces cerevisiae.Genetics · 2024Article
- An acidic loop in the FHA domain of the yeast meiosis-specific kinase Mek1 interacts with a specific motif in a subset of Mek1 substrates.bioRxiv : the preprint server for biology · 2024Article
- Qualitative rather than quantitative phosphoregulation shapes the end of meiosis I in budding yeast.The EMBO journal · 2024Article
- Rewiring of the phosphoproteome executes two meiotic divisions in budding yeast.The EMBO journal · 2024Article
- Systems level analysis of time and stimuli specific signaling through PKA.Molecular biology of the cell · 2024Article
- Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail.Nature communications · 2024Article
- CDK signaling via nonconventional CDK phosphorylation sites.Molecular biology of the cell · 2023Review
- Spo13/MEIKIN ensures a Two-Division meiosis by preventing the activation of APC/CThe EMBO journal · 2023Article
- Cla4 phosphorylates histone methyltransferase Set1 to prevent its degradation by the APC/CScience advances · 2023Article
166 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
28 authors at 7 institutions in 3 countries.
Funding
Abstract
Phosphorylation is a universal mechanism for regulating cell behavior in eukaryotes. Although protein kinases target short linear sequence motifs on their substrates, the rules for kinase substrate recognition are not completely understood. We used a rapid peptide screening approach to determine consensus phosphorylation site motifs targeted by 61 of the 122 kinases in Saccharomyces cerevisiae. By correlating these motifs with kinase primary sequence, we uncovered previously unappreciated rules for determining specificity within the kinase family, including a residue determining P-3 arginine specificity among members of the CMGC [CDK (cyclin-dependent kinase), MAPK (mitogen-activated protein kinase), GSK (glycogen synthase kinase), and CDK-like] group of kinases. Furthermore, computational scanning of the yeast proteome enabled the prediction of thousands of new kinase-substrate relationships. We experimentally verified several candidate substrates of the Prk1 family of kinases in vitro and in vivo and identified a protein substrate of the kinase Vhs1. Together, these results elucidate how kinase catalytic domains recognize their phosphorylation targets and suggest general avenues for the identification of previously unknown kinase substrates across eukaryotes.
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Registered trials
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.