SAPAPs
Open accessAbstract
PSD-95/SAP90 is a member of membrane-associated guanylate kinases localized at postsynaptic density (PSD) in neuronal cells. Membrane-associated guanylate kinases are a family of signaling molecules expressed at various submembrane domains which have the PDZ (DHR) domains, the SH3 domain, and the guanylate kinase domain. PSD-95/SAP90 interacts with N-methyl-D-aspartate receptors 2A/B, Shaker-type potassium channels, and brain nitric oxide synthase through the PDZ (DHR) domains and clusters these molecules at synaptic junctions. However, neither the function of the SH3 domain or the guanylate kinase domain of PSD-95/SAP90, nor the protein interacting with these domains has been identified. We have isolated here a novel protein family consisting of at least four members which specifically interact with PSD-95/SAP90 and its related proteins through the guanylate kinase domain, and named these proteins SAPAPs (SAP90/PSD-95-Associated Proteins). SAPAPs are specifically expressed in neuronal cells and enriched in the PSD fraction. SAPAPs induce the enrichment of PSD-95/SAP90 to the plasma membrane in transfected cells. Thus, SAPAPs may have a potential activity to maintain the structure of PSD by concentrating its components to the membrane area.
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Shank family proteins bind SAPAP directly to form the PSD95/SAPAP/Shank complex.
“Shank family proteins (Shank1–3) directly bind SAPAP to form the PSD95/SAPAP/Shank complex14,15.”
From Shank3 mutant mice display autistic-like behaviours and striatal dysfunction (2011) · cites this paper as [15]
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References 42 · Cited by 359
Research works printed but not linked: 6
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- Authors
- Takeuchi, M., Hata, Y., Hirao, K., Toyoda, A., Irie, M., & Takai, Y.
- Affiliations
- JCR Pharmaceuticals (Japan) (JP)
- Corresponding author
- Takai, Yoshimi
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-05
- Volume
- 272
- Issue
- 18
- Pages
- 11943-11951
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2018229588
- Cited by
- 359
- References
- 42
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 5 · 2022: 9 · 2021: 6 · 2020: 5 · 2019: 11 · 2018: 11 · 2017: 11 · 2016: 13 · 2015: 10 · 2014: 13 · 2013: 9 · 2012: 23
- FWCI
- 14.18
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- University of Washington
- Exploratory Research for Advanced Technology
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- PSD-95, membrane-associated guanylate kinase, postsynaptic density, guanylate kinase domain, protein-protein interaction, plasma membrane localization, neurons, NMDA receptor, Shaker potassium channel, nitric oxide synthase
- MeSH terms
- SAP90-PSD95 Associated Proteins, Disks Large Homolog 4 Protein, Amino Acid Sequence, Animals, Binding Sites, Brain, Cloning, Molecular, Kinetics, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Nucleoside-Phosphate Kinase, Recombinant Proteins, Synapses, Transfection, Potassium Channels, Gene Library, Receptors, N-Methyl-D-Aspartate, Sequence Homology, Amino Acid, DNA, Complementary, Nitric Oxide Synthase, COS Cells, Intracellular Signaling Peptides and Proteins, Rats, Guanylate Kinases, Shaker Superfamily of Potassium Channels
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