ArticleMolecular systems biology2023
Large-scale phosphomimetic screening identifies phospho-modulated motif-based protein interactions.
Article in Molecular systems biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Design and optimization of a kinase-controlled allosteric switch.Nature methods · 2026Article
- Technologies to measure and modulate protein subcellular localization.Nature reviews. Molecular cell biology · 2026Review
- Crystal structures reveal phosphorylation-dependent disruption of the heat shock protein 70-CHIP interface: A compensatory G132N variant restores binding affinity.Cell stress & chaperones · 2026Article
- FAM122A inhibition of PP2A-B55 through a bipartite binding mechanism.bioRxiv : the preprint server for biology · 2026Article
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- A proteome-wide biochemical screen defines binding determinants of the core autophagy protein LC3B.bioRxiv : the preprint server for biology · 2026Article
- A structural machine learning approach for rapid prediction of thermodynamically destabilizing tyrosine phosphorylations.Cell reports methods · 2025Article
- Decoding phospho-regulation and flanking regions in autophagy-associated short linear motifs.Communications biology · 2025Article
- Defining short linear motif binding determinants by phage display-based deep mutational scanning.Protein science : a publication of the Protein Society · 2025Article
- The LC3-interacting region of NBR1 is a protein interaction hub enabling optimal flux.The Journal of cell biology · 2025Article
- Opposing roles of p38α-mediated phosphorylation and PRMT1-mediated arginine methylation in driving TDP-43 proteinopathy.Cell reports · 2025Article
- Rapid prediction of thermodynamically destabilizing tyrosine phosphorylations in cancers.bioRxiv : the preprint server for biology · 2024Article
- Proteome-scale characterisation of motif-based interactome rewiring by disease mutations.Molecular systems biology · 2024Article
- [Relationship between GTSE1 and Cell Cycle and Potential Regulatory Mechanisms in Lung Cancer Cells].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2024Review
- The LC3-interacting region of NBR1 is a protein interaction hub enabling optimal flux.bioRxiv : the preprint server for biology · 2024Article
- Pathogenic mutations of human phosphorylation sites affect protein-protein interactions.Nature communications · 2024Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Large-scale phosphomimetic screening identifies phospho-modulated motif-based protein interactions.Molecular systems biology · 2023Article
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8 authors.
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Abstract
Phosphorylation is a ubiquitous post-translation modification that regulates protein function by promoting, inhibiting or modulating protein-protein interactions. Hundreds of thousands of phosphosites have been identified but the vast majority have not been functionally characterised and it remains a challenge to decipher phosphorylation events modulating interactions. We generated a phosphomimetic proteomic peptide-phage display library to screen for phosphosites that modulate short linear motif-based interactions. The peptidome covers ~13,500 phospho-serine/threonine sites found in the intrinsically disordered regions of the human proteome. Each phosphosite is represented as wild-type and phosphomimetic variant. We screened 71 protein domains to identify 248 phosphosites that modulate motif-mediated interactions. Affinity measurements confirmed the phospho-modulation of 14 out of 18 tested interactions. We performed a detailed follow-up on a phospho-dependent interaction between clathrin and the mitotic spindle protein hepatoma-upregulated protein (HURP), demonstrating the essentiality of the phospho-dependency to the mitotic function of HURP. Structural characterisation of the clathrin-HURP complex elucidated the molecular basis for the phospho-dependency. Our work showcases the power of phosphomimetic ProP-PD to discover novel phospho-modulated interactions required for cellular function.
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