ArticleThe Journal of biological chemistry2011
The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 71 citations in OpenAlex.
- A direct interaction of JAM-C with the tight junction scaffold protein ZO-2.Scientific reports · 2026Article
- Article
- The Role of ZO-2 in Modulating JAM-A and γ-Actin Junctional Recruitment, Apical Membrane and Tight Junction Tension, and Cell Response to Substrate Stiffness and Topography.International journal of molecular sciences · 2024Article
- Review
- Role of short chain fatty acids in gut health and possible therapeutic approaches in inflammatory bowel diseases.World journal of clinical cases · 2022Review
- Article
- Epithelial integrity, junctional complexes, and biomarkers associated with intestinal functions.Tissue barriers · 2022Review
- The F11 Receptor (F11R)/Junctional Adhesion Molecule-A (JAM-A) (F11R/JAM-A) in cancer progression.Molecular and cellular biochemistry · 2022Review
- Tandem Mass Tag Analysis of the Effect of the Anterior Cingulate Cortex in Nonerosive Reflux Disease Rats with Shugan Jiangni Hewei Granules Treatment.Computational and mathematical methods in medicine · 2022Article
- Junctional Adhesion Molecules: Potential Proteins in Atherosclerosis.Frontiers in cardiovascular medicine · 2022Review
- The order of PDZ3 and TrpCage in fusion chimeras determines their properties-a biophysical characterization.Protein science : a publication of the Protein Society · 2021Article
- The Epithelial Cell Leak Pathway.International journal of molecular sciences · 2021Review
- The Dual PDZ Domain from Postsynaptic Density Protein 95 Forms a Scaffold with Peptide Ligand.Biophysical journal · 2020Article
- Proteomic analysis of desmosomes reveals novel components required for epidermal integrity.Molecular biology of the cell · 2020Article
- Functional interplay between protein domains in a supramodular structure involving the postsynaptic density protein PSD-95.The Journal of biological chemistry · 2020Article
- Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and ZO-1 Expression in Rat Kidney Accompanied by Impaired Proximal Tubular Development.Oxidative medicine and cellular longevity · 2020Article
- Structural Features of Tight-Junction Proteins.International journal of molecular sciences · 2019Review
- Role of JAM-A tyrosine phosphorylation in epithelial barrier dysfunction during intestinal inflammation.Molecular biology of the cell · 2019Article
- VCAM-1 induces signals that stimulate ZO-1 serine phosphorylation and reduces ZO-1 localization at lung endothelial cell junctions.Journal of leukocyte biology · 2018Article
- Junctional adhesion molecule-A: functional diversity through molecular promiscuity.Cellular and molecular life sciences : CMLS · 2018Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Tight junctions are cell-cell contacts that regulate the paracellular flux of solutes and prevent pathogen entry across cell layers. The assembly and permeability of this barrier are dependent on the zonula occludens (ZO) membrane-associated guanylate kinase (MAGUK) proteins ZO-1, -2, and -3. MAGUK proteins are characterized by a core motif of protein-binding domains that include a PDZ domain, a Src homology 3 (SH3) domain, and a region of homology to guanylate kinase (GUK); the structure of this core motif has never been determined for any MAGUK. To better understand how ZO proteins organize the assembly of protein complexes we have crystallized the entire PDZ3-SH3-GUK core motif of ZO-1. We have also crystallized this core motif in complex with the cytoplasmic tail of the ZO-1 PDZ3 ligand, junctional adhesion molecule A (JAM-A) to determine how the activity of different domains is coordinated. Our study shows a new feature for PDZ class II ligand binding that implicates the two highly conserved Phe(-2) and Ser(-3) residues of JAM. Our x-ray structures and NMR experiments also show for the first time a role for adjacent domains in the binding of ligands to PDZ domains in the MAGUK proteins family.
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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.