ArticleJournal of molecular biology2011
Biochemical and structural characterization of β-catenin interactions with nonphosphorylated and CK2-phosphorylated Lef-1.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 54 citations in OpenAlex.
- Mutational scanning reveals substrate-assisted autoregulation of the WNT destruction complex.Nature genetics · 2026Article
- CRISPR-Cas9 Screening Identifies Resistance Mechanisms to KRAS Inhibition in Pancreatic Cancer.Cancer research · 2026Article
- Nuclear β-catenin: molecular regulation, challenges and therapeutic opportunities.Cell communication and signaling : CCS · 2025Review
- 15,16-Dihydrotanshinone I, a novel β-catenin-targeting inhibitor that inhibits its nuclear translocation and reduces downstream CD36 expression in cancer.Journal of translational medicine · 2025Article
- Mutational scanning reveals substrate-assisted autoregulation of the WNT destruction complex.bioRxiv : the preprint server for biology · 2025Article
- Design of target specific peptide inhibitors using generative deep learning and molecular dynamics simulations.Nature communications · 2024Article
- Gene-regulation modules in nonalcoholic fatty liver disease revealed by single-nucleus ATAC-seq.Life science alliance · 2023Article
- Phosphomevalonate Kinase Controls β-Catenin Signaling via the Metabolite 5-Diphosphomevalonate.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Lateral confined growth of cells activates Lef1 dependent pathways to regulate cell-state transitions.Scientific reports · 2022Article
- Article
- Structural overview and perspectives of the nuclear receptors, a major family as the direct targets for small-molecule drugs.Acta biochimica et biophysica Sinica · 2022Article
- Discovery of an Orally Bioavailable Small-Molecule Inhibitor for the β-Catenin/B-Cell Lymphoma 9 Protein-Protein Interaction.Journal of medicinal chemistry · 2021Article
- Direct targeting of β-catenin in the Wnt signaling pathway: Current progress and perspectives.Medicinal research reviews · 2021Review
- Parallel and Sequential Pathways of Molecular Recognition of a Tandem-Repeat Protein and Its Intrinsically Disordered Binding Partner.Biomolecules · 2021Article
- Elucidating the protein substrate recognition of O-GlcNAc transferase (OGT) toward O-GlcNAcase (OGA) using a GlcNAc electrophilic probe.International journal of biological macromolecules · 2021Article
- The structural biology of canonical Wnt signalling.Biochemical Society transactions · 2020Review
- Current View on EpCAM Structural Biology.Cells · 2020Review
- Macrocyclic peptides that inhibit Wnt signallingRSC chemical biology · 2020Article
- Optimization of Peptidomimetics as Selective Inhibitors for the β-Catenin/T-Cell Factor Protein-Protein Interaction.Journal of medicinal chemistry · 2019Article
- A novel cell-penetrating peptide suppresses breast tumorigenesis by inhibiting β-catenin/LEF-1 signaling.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In the Wnt/β-catenin signaling pathway, β-catenin activates target genes through its interactions with the T-cell factor/lymphoid enhancer-binding factor (TCF/Lef) family of transcription factors. The crystal structures of complexes between the β-catenin armadillo domain and the Lef-1 N-terminal domain show that the overall conformation and many of the interactions are similar to other published structures of TCFs bound to β-catenin. However, a second salt bridge in other TCF-β-catenin structures is absent in the structure of β-catenin-Lef-1 complex, indicating that this feature is not obligatory for β-catenin binding. Casein kinase II (CK2) has been shown to act as a positive regulator of Wnt signaling, and Lef-1 is a substrate of CK2. In vitro phosphorylation of purified Lef-1 was used to examine the effect of CK2 on the interaction of Lef-1 with β-catenin. Mass spectrometry data show that CK2 phosphorylation of Lef-1 N-terminal domain results in a single phosphorylation site at Ser40. Isothermal titration calorimetry revealed that β-catenin binds to nonphosphorylated or CK2-phosphorylated Lef-1 with the same affinity, which is consistent with the absence of phospho-Ser40 interactions in the crystal structure of phosphorylated Lef-1 N-terminal domain bound to β-catenin. These data indicate that the effect of CK2 on the Wnt/β-catenin pathway does not appear to be at the level of the Lef-1-β-catenin interaction.
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Registered trials
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.