ArticleJournal of molecular biology2019
Rewiring of RSK-PDZ Interactome by Linear Motif Phosphorylation.
Article in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
- Structural insights and biophysical characterization of p90RSK2:ERK2 complex.The Biochemical journal · 2025Article
- Discovery of effectors for casein kinase signaling in the African trypanosome.Scientific reports · 2025Article
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- Promiscuity mapping of the S100 protein family using a high-throughput holdup assay.Scientific reports · 2022Article
- Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs.The Biochemical journal · 2022Review
- Host PDZ-containing proteins targeted by SARS-CoV-2.The FEBS journal · 2021Article
- Noncanonical Sequences Involving NHERF1 Interaction with NPT2A Govern Hormone-Regulated Phosphate Transport: Binding Outside the Box.International journal of molecular sciences · 2021Review
- Phosphorylation-induced changes in the PDZ domain of Dishevelled 3.Scientific reports · 2021Article
- Integrated analysis of Shank1 PDZ interactions with C-terminal and internal binding motifs.Current research in structural biology · 2021Article
- Dynamic Control of Signaling by Phosphorylation of PDZ Binding Motifs.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Structural characterization and computational analysis of PDZ domains in Monosiga brevicollis.Protein science : a publication of the Protein Society · 2020Article
- Article
- Specificity in PDZ-peptide interaction networks: Computational analysis and review.Journal of structural biology: X · 2020Review
- Post-translational modifications of Drosophila melanogaster HOX protein, Sex combs reduced.PloS one · 2020Article
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
Abstract
Phosphorylation of short linear peptide motifs is a widespread process for the dynamic regulation of protein-protein interactions. However, the global impact of phosphorylation events on the protein-protein interactome is rarely addressed. The disordered C-terminal tail of ribosomal S6 kinase 1 (RSK1) binds to PDZ domain-containing scaffold proteins, and it harbors a phosphorylatable PDZ-binding motif (PBM) responsive to epidermal growth factor stimulation. Here, we examined binding of two versions of the RSK1 PBM, either phosphorylated or unphosphorylated at position -3, to almost all (95%) of the 266 PDZ domains of the human proteome. PBM phosphorylation dramatically altered the PDZ domain-binding landscape of RSK1, by strengthening or weakening numerous interactions to various degrees. The RSK-PDZome interactome analyzed in this study reveals how linear motif-based phospho-switches convey stimulus-dependent changes in the context of related network components.
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Registered trials
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