ArticleThe Journal of biological chemistry2014
Functional analysis of dishevelled-3 phosphorylation identifies distinct mechanisms driven by casein kinase 1ϵ and frizzled5.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 69 citations in OpenAlex.
- A Wnt-induced conformational phospho-switch in DVL3 controls association with Frizzled receptors and Wnt/β-catenin signaling.Science advances · 2026Article
- Gut microbiome-produced bile acid metabolite lengthens the circadian period in host intestinal cells.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Coupling mathematical modeling with a novel human intestinal stem cell system to understand feedback regulation during planar cell polarity.bioRxiv : the preprint server for biology · 2025Article
- WNT-induced association of Frizzled and LRP6 is not sufficient for the initiation of WNT/β-catenin signaling.Nature communications · 2025Article
- Frizzled receptors: gatekeepers of Wnt signaling in development and disease.Frontiers in cell and developmental biology · 2025Review
- Review
- Carboxy-terminal polyglutamylation regulates signaling and phase separation of the Dishevelled protein.The EMBO journal · 2024Article
- A phosphorylation-controlled switch confers cell cycle-dependent protein relocalization.Nature cell biology · 2024Article
- Efficient cloning of linear DNA inserts (ECOLI) into plasmids using site-directed mutagenesis.Scientific reports · 2024Article
- A phosphorylation-controlled switch confers cell cycle-dependent protein relocalization.bioRxiv : the preprint server for biology · 2024Article
- Role of the Ror family receptors in Wnt5a signaling.In vitro cellular & developmental biology. Animal · 2024Review
- Disheveled-1 Interacts with Claudin-5 and Contributes to Norrin-Induced Endothelial Barrier Restoration.Cells · 2023Article
- Pathway selectivity in Frizzleds is achieved by conserved micro-switches defining pathway-determining, active conformations.Nature communications · 2023Article
- The conserved Pelado/ZSWIM8 protein regulates actin dynamics by promoting linear actin filament polymerization.Life science alliance · 2022Article
- Article
- Regulation of Dishevelled DEP domain swapping by conserved phosphorylation sites.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Phosphorylation-induced changes in the PDZ domain of Dishevelled 3.Scientific reports · 2021Article
- Intersection of two key signal integrators in the cell: activator of G-protein signaling 3 and dishevelled-2.Journal of cell science · 2020Article
- Single-molecule dynamics of Dishevelled at the plasma membrane and Wnt pathway activation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Activity of Smurf2 Ubiquitin Ligase Is Regulated by the Wnt Pathway Protein Dishevelled.Cells · 2020Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dishevelled-3 (Dvl3), a key component of the Wnt signaling pathways, acts downstream of Frizzled (Fzd) receptors and gets heavily phosphorylated in response to pathway activation by Wnt ligands. Casein kinase 1ϵ (CK1ϵ) was identified as the major kinase responsible for Wnt-induced Dvl3 phosphorylation. Currently it is not clear which Dvl residues are phosphorylated and what is the consequence of individual phosphorylation events. In the present study we employed mass spectrometry to analyze in a comprehensive way the phosphorylation of human Dvl3 induced by CK1ϵ. Our analysis revealed >50 phosphorylation sites on Dvl3; only a minority of these sites was found dynamically induced after co-expression of CK1ϵ, and surprisingly, phosphorylation of one cluster of modified residues was down-regulated. Dynamically phosphorylated sites were analyzed functionally. Mutations within PDZ domain (S280A and S311A) reduced the ability of Dvl3 to activate TCF/LEF (T-cell factor/lymphoid enhancer factor)-driven transcription and induce secondary axis in Xenopus embryos. In contrast, mutations of clustered Ser/Thr in the Dvl3 C terminus prevented ability of CK1ϵ to induce electrophoretic mobility shift of Dvl3 and its even subcellular localization. Surprisingly, mobility shift and subcellular localization changes induced by Fzd5, a Wnt receptor, were in all these mutants indistinguishable from wild type Dvl3. In summary, our data on the molecular level (i) support previous the assumption that CK1ϵ acts via phosphorylation of distinct residues as the activator as well as the shut-off signal of Wnt/β-catenin signaling and (ii) suggest that CK1ϵ acts on Dvl via different mechanism than Fzd5.
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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.