ArticleMolecular systems biology2022
A human kinase yeast array for the identification of kinases modulating phosphorylation-dependent protein-protein interactions.
Article in Molecular systems biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 18 citations in OpenAlex.
- Neurochondrin promotes U5 snRNP maturation by regulating AAR2 release from PRPF8.Nucleic acids research · 2026Article
- The allosteric landscape of the Src kinase.Science advances · 2026Article
- Uncovering the molecular basis of kinase activity and substrate recognition with phospho-PCA.bioRxiv : the preprint server for biology · 2025Article
- The fitness cost of spurious phosphorylation.The EMBO journal · 2024Article
- Reverse-Phase Protein Microarrays for OverexpressedAnalytical chemistry · 2024Article
- Structural basis of human U5 snRNP late biogenesis and recycling.Nature structural & molecular biology · 2024Article
- Illuminating the druggable genome: Pathways to progress.Drug discovery today · 2024Review
- The fitness cost of spurious phosphorylation.bioRxiv : the preprint server for biology · 2023Article
- Missense variant interaction scanning reveals a critical role of the FERM domain for tumor suppressor protein NF2 conformation and function.Life science alliance · 2023Article
- Article
- A human kinase yeast array for the identification of kinases modulating phosphorylation-dependent protein-protein interactions.Molecular systems biology · 2022Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Protein kinases play an important role in cellular signaling pathways and their dysregulation leads to multiple diseases, making kinases prime drug targets. While more than 500 human protein kinases are known to collectively mediate phosphorylation of over 290,000 S/T/Y sites, the activities have been characterized only for a minor, intensively studied subset. To systematically address this discrepancy, we developed a human kinase array in Saccharomyces cerevisiae as a simple readout tool to systematically assess kinase activities. For this array, we expressed 266 human kinases in four different S. cerevisiae strains and profiled ectopic growth as a proxy for kinase activity across 33 conditions. More than half of the kinases showed an activity-dependent phenotype across many conditions and in more than one strain. We then employed the kinase array to identify the kinase(s) that can modulate protein-protein interactions (PPIs). Two characterized, phosphorylation-dependent PPIs with unknown kinase-substrate relationships were analyzed in a phospho-yeast two-hybrid assay. CK2α1 and SGK2 kinases can abrogate the interaction between the spliceosomal proteins AAR2 and PRPF8, and NEK6 kinase was found to mediate the estrogen receptor (ERα) interaction with 14-3-3 proteins. The human kinase yeast array can thus be used for a variety of kinase activity-dependent readouts.
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