ArticleCell research2014
Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl.
Article in Cell research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed.
- Unveiling the Tumor Suppressors: Insights from Drosophila.Advances in experimental medicine and biology · 2025Review
- Article
- Phosphorylation-dependent recognition of diverse protein targets by the cryptic GK domain of MAGI MAGUKs.Science advances · 2023Article
- Minimal functional domains of the core polarity regulator Dlg.Biology open · 2022Article
- Application of per-Residue Energy Decomposition to Design Peptide Inhibitors of PSD95 GK Domain.Frontiers in molecular biosciences · 2022Article
- CeLINC, a fluorescence-based protein-protein interaction assay in Caenorhabditis elegans.Genetics · 2021Article
- Entropy of stapled peptide inhibitors in free state is the major contributor to the improvement of binding affinity with the GK domain.RSC chemical biology · 2021Article
- Scribble, Lgl1, and myosin II form a complex in vivo to promote directed cell migration.Molecular biology of the cell · 2020Article
- Breaking symmetry - cell polarity signaling pathways in growth cone guidance and synapse formation.Current opinion in neurobiology · 2020Review
- Distinct activities of Scrib module proteins organize epithelial polarity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Case of the Scribble Polarity Module in Asymmetric Neuroblast Division in Development and Tumorigenesis.International journal of molecular sciences · 2020Review
- Characterizing the Binding Sites for GK Domain of DLG1 and DLG4 via Molecular Dynamics Simulation.Frontiers in molecular biosciences · 2020Article
- Switching states: dynamic remodelling of polarity complexes as a toolkit for cell polarization.Current opinion in cell biology · 2019Review
- Scribble co-operatively binds multiple αScientific reports · 2019Article
- Solving the structure of Lgl2, a difficult blind test of unsupervised structure determination.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- PAR3-PAR6-atypical PKC polarity complex proteins in neuronal polarization.Cellular and molecular life sciences : CMLS · 2018Review
- Phosphoinositides and Membrane Targeting in Cell Polarity.Cold Spring Harbor perspectives in biology · 2018Review
- Proteasome-independent polyubiquitin linkage regulates synapse scaffolding, efficacy, and plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Development and dynamics of cell polarity at a glance.Journal of cell science · 2017Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The tumor suppressors Discs Large (Dlg), Lethal giant larvae (Lgl) and Scribble are essential for the establishment and maintenance of epithelial cell polarity in metazoan. Dlg, Lgl and Scribble are known to interact strongly with each other genetically and form the evolutionarily conserved Scribble complex. Despite more than a decade of extensive research, it has not been demonstrated whether Dlg, Lgl and Scribble physically interact with each other. Here, we show that Dlg directly interacts with Lgl in a phosphorylation-dependent manner. Phosphorylation of any one of the three conserved Ser residues situated in the central linker region of Lgl is sufficient for its binding to the Dlg guanylate kinase (GK) domain. The crystal structures of the Dlg4 GK domain in complex with two phosphor-Lgl2 peptides reveal the molecular mechanism underlying the specific and phosphorylation-dependent Dlg/Lgl complex formation. In addition to providing a mechanistic basis underlying the regulated formation of the Scribble complex, the structure of the Dlg/Lgl complex may also serve as a starting point for designing specific Dlg inhibitors for targeting the Scribble complex formation.
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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.