Binding of Neuroligins to PSD-95
Abstract
PSD-95 is a component of postsynaptic densities in central synapses. It contains three PDZ domains that localize N -methyl- d -aspartate receptor subunit 2 (NMDA2 receptor) and K + channels to synapses. In mouse forebrain, PSD-95 bound to the cytoplasmic COOH-termini of neuroligins, which are neuronal cell adhesion molecules that interact with β-neurexins and form intercellular junctions. Neuroligins bind to the third PDZ domain of PSD-95, whereas NMDA2 receptors and K + channels interact with the first and second PDZ domains. Thus different PDZ domains of PSD-95 are specialized for distinct functions. PSD-95 may recruit ion channels and neurotransmitter receptors to intercellular junctions formed between neurons by neuroligins and β-neurexins.
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PSD95-SAPAP-Shank proteins form a key postsynaptic scaffold at glutamatergic synapses that interacts with many synaptic proteins, including the Neurexin-Neuroligin complex.
“PSD95-SAPAP-Shank proteins form a key postsynaptic scaffold at glutamatergic synapses which interacts with many synaptic proteins including the Neurexin-Neuroligin complex25.”
From Shank3 mutant mice display autistic-like behaviours and striatal dysfunction (2011) · cites this paper as [25]
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- Authors
- Irie, M., Hata, Y., Takeuchi, M., Ichtchenko, K., Toyoda, A., Hirao, K., Takai, Y., Rosahl, T. W., & Südhof, T. C.
- Affiliations
- Howard Hughes Medical Institute (US)
- M. Irie, M. Takeuchi, A. Toyoda, K. Hirao, Takai Biotimer Project, ERATO, Japan Science and Technology Corporation, 2-2-10, Murotani, Nishi-ku, Kobe, 651-22, Japan. Y. Hata, Howard Hughes Medical Institute and Department of Molecular Genetics, University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75235–9050, USA, and Takai Biotimer Project, ERATO, Japan Science and Technology Corporation, 2-2-10, Murotani, Nishi-ku, Kobe 651-22, Japan.
- Venue
- Science
- Published
- 1997-09-05
- Volume
- 277
- Issue
- 5331
- Pages
- 1511-1515
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2015556634
- Cited by
- 749
- References
- 25
- Citations by year
- 2026: 9 · 2025: 18 · 2024: 12 · 2023: 21 · 2022: 23 · 2021: 12 · 2020: 22 · 2019: 22 · 2018: 24 · 2017: 18 · 2016: 23 · 2015: 23 · 2014: 22 · 2013: 30 · 2012: 31
- FWCI
- 19.19
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Mental Health (R01MH052804)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- neuroligins, PSD-95, PDZ domain, postsynaptic density, NMDA receptor, potassium channels, adhesion molecules, synaptogenesis, intercellular junctions, neurotransmitter receptors
- MeSH terms
- Disks Large Homolog 4 Protein, Amino Acid Sequence, Animals, Cell Line, Cell Membrane, Cytoplasm, Intercellular Junctions, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Nucleoside-Phosphate Kinase, Recombinant Fusion Proteins, Potassium Channels, Cell Adhesion Molecules, Neuronal, Receptors, N-Methyl-D-Aspartate, Prosencephalon, Calcium-Calmodulin-Dependent Protein Kinases, COS Cells, Tumor Suppressor Proteins, Intracellular Signaling Peptides and Proteins, Mice, Guanylate Kinases
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