ArticleProtein science : a publication of the Protein Society2009
Sequence requirement and subtype specificity in the high-affinity interaction between human frizzled and dishevelled proteins.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 47 citations in OpenAlex.
- Wnt/β-catenin signaling pathway: proteins' roles in osteoporosis and cancer diseases and the regulatory effects of natural compounds on osteoporosis.Molecular medicine (Cambridge, Mass.) · 2024Review
- Craniofacial studies in chicken embryos confirm the pathogenicity of human FZD2 variants associated with Robinow syndrome.Disease models & mechanisms · 2024Article
- Article
- Novel pathogenic variants and quantitative phenotypic analyses of Robinow syndrome: WNT signaling perturbation and phenotypic variability.HGG advances · 2022Article
- The Wnt signaling pathway in tumorigenesis, pharmacological targets, and drug development for cancer therapy.Biomarker research · 2021Review
- Small-molecule inhibitors of the PDZ domain of Dishevelled proteins interrupt Wnt signalling.Magnetic resonance (Gottingen, Germany) · 2021Article
- The Impact of Gut Microbiota Disorders on the Blood-Brain Barrier.Infection and drug resistance · 2020Review
- Dishevelled-3 conformation dynamics analyzed by FRET-based biosensors reveals a key role of casein kinase 1.Nature communications · 2019Article
- WNT Signaling Perturbations Underlie the Genetic Heterogeneity of Robinow Syndrome.American journal of human genetics · 2018Article
- Wnt Signalosome Assembly by DEP Domain Swapping of Dishevelled.Molecular cell · 2016Article
- Identification of the first small-molecule inhibitor of the REV7 DNA repair protein interaction.Bioorganic & medicinal chemistry · 2016Article
- Frizzled-4 C-terminus Distal to KTXXXW Motif is Essential for Normal Dishevelled Recruitment and Norrin-stimulated Activation of Lef/Tcf-dependent Transcriptional Activation.Journal of molecular signaling · 2016Article
- The Intracellular Loop 2 F328S Frizzled-4 Mutation Implicated in Familial Exudative Vitreoretinopathy Impairs Dishevelled Recruitment.Journal of molecular signaling · 2015Article
- Molecular Role of RNF43 in Canonical and Noncanonical Wnt Signaling.Molecular and cellular biology · 2015Article
- Silencing dishevelled-1 sensitizes paclitaxel-resistant human ovarian cancer cells via AKT/GSK-3β/β-catenin signalling.Cell proliferation · 2015Article
- Shroom3 functions downstream of planar cell polarity to regulate myosin II distribution and cellular organization during neural tube closure.Biology open · 2015Article
- The Wnt/β-catenin pathway in human fibrotic-like diseases and its eligibility as a therapeutic target.Molecular and cellular therapies · 2015Article
- Development of anticancer agents targeting the Wnt/β-catenin signaling.American journal of cancer research · 2015Review
- The multifaceted role of CD146/MCAM in the promotion of melanoma progression.Cancer cell international · 2015Article
- WNT/Frizzled signalling: receptor-ligand selectivity with focus on FZD-G protein signalling and its physiological relevance: IUPHAR Review 3.British journal of pharmacology · 2014Review
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the Wnt family of lipoglycoproteins initiate signaling by binding to Frizzled (Fz) receptors, and the signal is then relayed by Disheveled (Dvl). The Dvl PDZ domain is known to interact directly with a peptide derived from the KTXXXW motif of Fz7, which is conserved in all known Fz subtypes. We found that an extended region spanning the KTXXXW motif on both its N-terminal and C-terminal sides dramatically influences the affinity of peptides derived from Fz7 for Dvl PDZ. An alanine scanning study identified the specific residues external to the KTXXXW motif that are important for high-affinity binding. In a circular dichroism analysis, mutation of some of these critical residues resulted in peptide conformational changes, suggesting that the secondary structure of the peptides contributes to Fz-Dvl PDZ binding. Of the 10 known Fz subtypes, peptides derived from only Fz1, Fz2, Fz3, Fz4, and Fz7 directly bound to Dvl PDZ domain in our study. Other Fz subtypes, including some known to be involved in Wnt/beta-catenin signaling (Fz5, Fz9), did not bind to Dvl, suggesting that direct interaction with Dvl PDZ does not determine the subtype-specific functionality of Fz. Molecular modeling and circular dichroism studies indicated that the Fz peptides that bind to Dvl PDZ domain form specific conformations that are different from those of nonbinding peptides.
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