ArticleThe Journal of biological chemistry2011
The structure of the PDZ3-SH3-GuK tandem of ZO-1 protein suggests a supramodular organization of the membrane-associated guanylate kinase (MAGUK) family scaffold protein core.
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 30 papers.
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Who cites it
30 citing papers in PubMed, 57 citations in OpenAlex.
- A direct interaction of JAM-C with the tight junction scaffold protein ZO-2.Scientific reports · 2026Article
- Molecular Dynamics and Docking Reveal Enhanced Binding of HPV16 E6 Asian American Variants To non-phosphorylated DLG1.Cell biochemistry and biophysics · 2026Article
- Diurnal testosterone oscillations gate drug delivery via phase separation of ZO-1 at the blood-testis barrier in mice.Communications biology · 2026Article
- Visualizing Postsynaptic Density in Excitatory Synapses with Electron Tomography.Advances in neurobiology · 2026Review
- PSD-95: An Effective Target for Stroke Therapy Using Neuroprotective Peptides.International journal of molecular sciences · 2021Review
- The order of PDZ3 and TrpCage in fusion chimeras determines their properties-a biophysical characterization.Protein science : a publication of the Protein Society · 2021Article
- Exosomal delivery of therapeutic modulators through the blood-brain barrier; promise and pitfalls.Cell & bioscience · 2021Review
- Divergent Evolution of a Protein-Protein Interaction Revealed through Ancestral Sequence Reconstruction and Resurrection.Molecular biology and evolution · 2021Article
- A novel cell-penetrating peptide targeting calpain-cleavage of PSD-95 induced by excitotoxicity improves neurological outcome after stroke.Theranostics · 2021Article
- Article
- The PDZ motif peptide of ZO-1 attenuates Pseudomonas aeruginosa LPS-induced airway inflammation.Scientific reports · 2020Article
- Phase separation as a therapeutic target in tight junction-associated human diseases.Acta pharmacologica Sinica · 2020Review
- Functional interplay between protein domains in a supramodular structure involving the postsynaptic density protein PSD-95.The Journal of biological chemistry · 2020Article
- Understanding the Molecular and Cell Biological Mechanisms of Electrical Synapse Formation.Frontiers in neuroanatomy · 2020Article
- Protein painting, an optimized MS-based technique, reveals functionally relevant interfaces of the PD-1/PD-L1 complex and the YAP2/ZO-1 complex.The Journal of biological chemistry · 2019Article
- PDZ Domains as Drug Targets.Advanced therapeutics · 2019Review
- Seeking allosteric networks in PDZ domains.Protein engineering, design & selection : PEDS · 2018Review
- Two microcephaly-associated novel missense mutations in CASK specifically disrupt the CASK-neurexin interaction.Human genetics · 2018Article
- Article
- Defenders and Challengers of Endothelial Barrier Function.Frontiers in immunology · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane-associated guanylate kinases (MAGUKs) are a large family of scaffold proteins that play essential roles in tethering membrane receptors, adhesion molecules, and macromolecular signaling complexes for tissue developments, cell-cell communications, and intracellular signal transductions. The defining feature of the MAGUK family scaffolds is that each member contains a conserved core consisting of a PSD-95/Dlg/ZO-1 (PDZ) domain, an Src homology 3 (SH3) domain, and a catalytically inactive guanylate kinase (GuK) domain arranged in tandem, although the structural features and functional implications of the PDZ-SH3-GuK tandem arrangement are unclear. The structure of the ZO-1 PDZ3-SH3-GuK tandem solved in this study reveals that the PDZ domain directly interacts with the SH3-GuK module, forming a structural supramodule with distinct target binding properties with respect to the isolated domains. Structure-based sequence analysis suggests that the PDZ-SH3-GuK tandems of other members of the MAGUK family also form supramodules.
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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.