The DOI matches its Crossref record; 61 of the 62 references it cites were found in a registry or an index.
Coordinated PKA and PKC phosphorylation suppresses RXR-mediated ER retention and regulates the surface delivery of NMDA receptors
Abstract
Endoplasmic reticulum (ER) retention mediated by the RXR (Arg-X-Arg) motif is an important quality control mechanism used by G-protein coupled receptors and ion channels, including N-methyl-D-aspartate (NMDA) receptors, to ensure the proper assembly and trafficking of multimeric complexes. During assembly, RXR motifs are masked by intersubunit interactions thereby allowing ER release. Here, we find that PKA and PKC phosphorylation sites flanking the RXR motif of the NMDA receptor NR1 subunit suppress ER retention and regulate receptor forward trafficking. These sites are differentially phosphorylated during the trafficking of NR1 subunits in vivo, and phosphorylation at these sites occurs in early secretory compartments. In addition, residues near the RXR motif not involved in phosphorylation are also required for ER retention. These results indicate that ER retention of NMDA receptors is tightly regulated, and suggest that coordinated phosphorylation by PKA and PKC mediates release of receptors from the ER for subsequent traffic to synapses. Phosphorylation-induced ER export of RXR-containing channels and receptors may serve as a novel quality control mechanism for creating a readily releasable pool of receptors sensitive to the activation of intracellular signaling pathways.
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“RXR motifs enhance the ER localization of ion channels (Scott et al., 2003; Gassmann et al., 2005).”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Scott et al., 2003
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Glutamate Receptor Ion Channels: Structure, Regulation, and Function
Traynelis, S. F., Wollmuth, L. P., McBain, C. J., Menniti, F. S., Vance, K. M., Ogden, K. K., Hansen, K. B., Yuan, H., Myers, S. J., & Dingledine, R. (2010) · Pharmacological Reviews · doi:10.1124/pr.109.002451 · Cited by 3,568
NMDA receptor trafficking in synaptic plasticity and neuropsychiatric disorders
Lau, C. G., & Zukin, R. S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2153 · Cited by 1,159
Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000131 · Cited by 686
Structure, function, and allosteric modulation of NMDA receptors
Hansen, K. B., Yi, F., Perszyk, R. E., Furukawa, H., Wollmuth, L. P., Gibb, A. J., & Traynelis, S. F. (2018) · The Journal of General Physiology · doi:10.1085/jgp.201812032 · Cited by 612
Metadata
- Authors
- Scott, D. B., Blanpied, T. A., & Ehlers, M. D.
- Affiliations
- Duke Medical Center (US)
- Duke University (US)
- Corresponding author
- Ehlers, Michael D.
- Venue
- Neuropharmacology
- Publisher
- Elsevier BV
- Published
- 2003-11
- Volume
- 45
- Issue
- 6
- Pages
- 755-767
- ISSN
- 0028-3908 (ISSN-L)
- OpenAlex
- W2052488789
- Cited by
- 186
- References
- 62
- Citations by year
- 2025: 2 · 2024: 3 · 2023: 2 · 2022: 7 · 2021: 5 · 2020: 5 · 2019: 3 · 2018: 7 · 2017: 8 · 2016: 6 · 2015: 6 · 2014: 7 · 2013: 9 · 2012: 6
- FWCI
- 4.04
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuropharmacology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Alcohol Abuse and Alcoholism (F31 AA13220, F31AA013220)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- NMDA receptor, NR1 subunit, endoplasmic reticulum retention, protein kinase A, protein kinase C, phosphorylation, receptor trafficking, ER export, quality control, G protein-coupled receptors, ion channels
- MeSH terms
- Amino Acid Sequence, Animals, Arginine, Cell Membrane, Chlorocebus aethiops, Endoplasmic Reticulum, Humans, Molecular Sequence Data, Neurons, Phosphorylation, Protein Kinase C, Receptors, N-Methyl-D-Aspartate, Cyclic AMP-Dependent Protein Kinases, COS Cells, Amino Acid Motifs, Rats
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