Cited by 418Neuroscience and Neuropharmacology ResearchCellular transport and secretionReceptor Mechanisms and Signaling

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An NMDA Receptor ER Retention Signal Regulated by Phosphorylation and Alternative Splicing

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Scott, Derek B., Blanpied, Thomas A., Swanson, Geoffrey T., Zhang, Chi, Ehlers, Michael D.·2001·The Journal of Neuroscience

DOI 10.1523/jneurosci.21-09-03063.2001PMC PMC6762585

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Abstract

Formation of mature excitatory synapses requires the assembly and delivery of NMDA receptors to the neuronal plasma membrane. A key step in the trafficking of NMDA receptors to synapses is the exit of newly assembled receptors from the endoplasmic reticulum (ER). Here we report the identification of an RXR-type ER retention/retrieval motif in the C-terminal tail of the NMDA receptor subunit NR1 that regulates receptor surface expression in heterologous cells and in neurons. In addition, we show that PKC phosphorylation and an alternatively spliced consensus type I PDZ-binding domain suppress ER retention. These results demonstrate a novel quality control function for alternatively spliced C-terminal domains of NR1 and implicate both phosphorylation and potential PDZ-mediated interactions in the trafficking of NMDA receptors through early stages of the secretory pathway.

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Retracted
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Authors: Scott, D. B., Blanpied, T. A., Swanson, G. T., Zhang, C., & Ehlers, M. D.
Affiliations: Duke Medical Center (US)
Salk Institute for Biological Studies (US)
ORCID: Blanpied, Thomas A.
Swanson, Geoffrey T.
Zhang, Chi
Ehlers, Michael D.
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2001-05-01
Volume: 21
Issue: 9
Pages: 3063-3072
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.21-09-03063.2001
PMC: PMC6762585
OpenAlex: W1527134354
Cited by: 418
References: 62
Citations by year: 2026: 4 · 2025: 5 · 2024: 5 · 2023: 5 · 2022: 10 · 2021: 10 · 2020: 10 · 2019: 8 · 2018: 11 · 2017: 10 · 2016: 3 · 2015: 12 · 2014: 13 · 2013: 10 · 2012: 10
FWCI: 12.93
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 184 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Alfred P. Sloan Foundation
American Health Assistance Foundation
McKnight Foundation
North Carolina Biotechnology Center
Triangle Community Foundation
National Alliance for Research on Schizophrenia and Depression
National Institutes of Health
National Institute of Neurological Disorders and Stroke (R01 NS39402, R01NS039402)
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 › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: NMDA receptor, NR1 subunit, endoplasmic reticulum retention signal, PKC phosphorylation, alternative splicing, PDZ-binding domain, receptor surface expression, excitatory synapse formation, secretory pathway, quality control, receptor trafficking
MeSH terms: Animals, Cells, Cultured, Endoplasmic Reticulum, Hippocampus, Humans, Neurons, Phosphorylation, Protein Kinase C, Recombinant Fusion Proteins, Transcription Factors, Transfection, Receptors, Interleukin-2, Receptors, N-Methyl-D-Aspartate, Alternative Splicing, Protein Structure, Tertiary, Receptors, Retinoic Acid, Amino Acid Motifs, Protein Subunits, Protein Sorting Signals, Retinoid X Receptors, Rats

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An NMDA Receptor ER Retention Signal Regulated by Phosphorylation and Alternative Splicing

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