ArticleThe Journal of biological chemistry2007
Domain swapping within PDZ2 is responsible for dimerization of ZO proteins.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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Who cites it
39 citing papers in PubMed, 59 citations in OpenAlex.
- Tight junction structure, assembly and (dys)function.Nature reviews. Molecular cell biology · 2026Review
- Homer condensates orchestrate YAP-Wnt signaling crosstalk downstream of the Crumbs polarity complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A direct interaction of JAM-C with the tight junction scaffold protein ZO-2.Scientific reports · 2026Article
- Defining the human lung pathodegradome of the V8 protease fromInfection and immunity · 2026Article
- The relationship between Connexin 43 (Cx43) and partner protein, human discs large homologue-1 (Dlg1) during wound closure in keratinocytes.Cell and tissue research · 2026Article
- HTRF-based identification of small molecules targeting SARS-CoV-2 E protein interaction with ZO-1 PDZ2.Scientific reports · 2025Article
- Protection of Tight Junctional Complexes between hCMEC/D3 Cells by Deep-Sea Fibrinolytic Compound FGFC1.Marine drugs · 2024Article
- PDZ2-conjugated-PLGA nanoparticles are tiny heroes in the battle against SARS-CoV-2.Scientific reports · 2024Article
- The Basic Requirement of Tight Junction Proteins in Blood-Brain Barrier Function and Their Role in Pathologies.International journal of molecular sciences · 2024Review
- Monomeric and dimeric states of human ZO1-PDZ2 are functional partners of the SARS-CoV-2 E protein.Computational and structural biotechnology journal · 2023Article
- Epithelial integrity, junctional complexes, and biomarkers associated with intestinal functions.Tissue barriers · 2022Review
- Interactions of Severe Acute Respiratory Syndrome Coronavirus 2 Protein E With Cell Junctions and Polarity PSD-95/Dlg/ZO-1-Containing Proteins.Frontiers in microbiology · 2022Article
- Ruffles and spikes: Control of tight junction morphology and permeability by claudins.Biochimica et biophysica acta. Biomembranes · 2020Review
- Hidden kinetic traps in multidomain folding highlight the presence of a misfolded but functionally competent intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cardiomyocyte Expression of ZO-1 Is Essential for Normal Atrioventricular Conduction but Does Not Alter Ventricular Function.Circulation research · 2020Article
- Structural Features of Tight-Junction Proteins.International journal of molecular sciences · 2019Review
- PDZ Domains as Drug Targets.Advanced therapeutics · 2019Review
- Emerging Themes in PDZ Domain Signaling: Structure, Function, and Inhibition.International review of cell and molecular biology · 2019Review
- Prediction of Host-Pathogen Interactions for Helicobacter pylori by Interface Mimicry and Implications to Gastric Cancer.Journal of molecular biology · 2017Article
- Structural Basis of a Key Factor Regulating the Affinity between the Zonula Occludens First PDZ Domain and Claudins.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
ZO-1 is a multidomain protein involved in cell-cell junctions and contains three PDZ domains, which are necessary for its function in vivo. PDZ domains play a central role in assembling diverse protein complexes through their ability to recognize short peptide motifs on other proteins. We determined the structure of the second of the three PDZ domains of ZO-1, which is known to promote dimerization as well as bind to C-terminal sequences on connexins. The dimer is stabilized by extensive symmetrical domain swapping of beta-strands, which is unlike any other known mechanism of PDZ dimerization. The canonical peptide-binding groove remains intact in both subunits of the PDZ2 dimer and is created by elements contributed from both monomers. This unique structure reveals an additional example of how PDZ domains dimerize and has multiple implications for both peptide binding and oligomerization in vivo.
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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.