Scribble1/AP2 complex coordinates NMDA receptor endocytic recycling
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The appropriate trafficking of glutamate receptors to synapses is crucial for basic synaptic function and synaptic plasticity. It is now accepted that NMDA receptors (NMDARs) internalize and are recycled at the plasma membrane but also exchange between synaptic and extrasynaptic pools; these NMDAR properties are also key to governing synaptic plasticity. Scribble1 is a large PDZ protein required for synaptogenesis and synaptic plasticity. Herein, we show that the level of Scribble1 is regulated in an activity-dependent manner and that Scribble1 controls the number of NMDARs at the plasma membrane. Notably, Scribble1 prevents GluN2A subunits from undergoing lysosomal trafficking and degradation by increasing their recycling to the plasma membrane following NMDAR activation. Finally, we show that a specific YxxR motif on Scribble1 controls these mechanisms through a direct interaction with AP2. Altogether, our findings define a molecular mechanism to control the levels of synaptic NMDARs via Scribble1 complex signaling.
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Scribble directly binds NMDA receptor subunits GluN2A and GluN2B through PDZ2 and PDZ3 interactions and can also bind the clathrin-mediated endocytosis regulator AP2.
“Scribble directly binds NMDA receptor subunits GluN2A and GluN2B through PDZ2 and PDZ3 interactions and can also bind the clathrin-mediated endocytosis regulator AP2, which regulates NMDA receptor internalization (Piguel et al., 2014).”
From Scribble: A master scaffold in polarity, adhesion, synaptogenesis, and proliferation (2019) · cites this paper as Piguel et al., 2014
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“Scribble directly binds NMDA receptor subunits GluN2A and GluN2B through PDZ2 and PDZ3 interactions and can also bind the clathrin-mediated endocytosis regulator AP2, which regulates NMDA receptor internalization (Piguel et al., 2014).”
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Self-citation
- Authors
- Piguel, N. H., Fievre, S., Blanc, J.-M., Carta, M., Moreau, M. M., Moutin, E., Pinheiro, V. L., Medina, C., Ezan, J., Lasvaux, L., Loll, F., Durand, C. M., Chang, K., Petralia, R. S., Wenthold, R. J., Stephenson, F. A., Vuillard, L., Darbon, H., Perroy, J., Mulle, C., Montcouquiol, M., Racca, C., & Sans, N.
- Affiliations
- Université de Bordeaux (FR)
- Centre National de la Recherche Scientifique (FR)
- National Institutes of Health (US)
- UCL School of Pharmacy (GB)
- Newcastle University (GB)
- Corresponding author
- Sans, Nathalie
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 9
- Issue
- 2
- Pages
- 712-727
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2001248033
- Cited by
- 52
- References
- 47
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 3 · 2023: 1 · 2022: 5 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 7 · 2017: 8 · 2016: 7 · 2015: 1 · 2014: 4
- FWCI
- 3.05
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Oskar-Bordeaux (Universite de Bordeaux) (submittedVersion, cc-by-nc-nd)
- Newcastle University ePrints (Newcastle Univesity) (cc-by-nc-nd)
- Funders
- Royal Society
- Fondation pour la Recherche Médicale (ANR-07-NEUR-031-01, FDT20130928124, SPF20081215186)
- Newcastle University
- National Institutes of Health
- Wellcome Trust
- National Institute on Deafness and Other Communication Disorders
- Université de Bordeaux
- Conseil Régional Aquitaine
- Institut National de la Santé et de la Recherche Médicale
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- NMDA receptor, AP-2, lysosomal trafficking, synaptic plasticity, PDZ domain proteins, activity-dependent regulation, glutamate receptors
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Cells, Cultured, Molecular Sequence Data, Neurons, Protein Binding, Endosomes, Receptors, N-Methyl-D-Aspartate, Rats, Sprague-Dawley, Amino Acid Motifs, Protein Transport, Tumor Suppressor Proteins, Adaptor Protein Complex 2, Rats, Proteolysis
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