The DOI matches its Crossref record; 127 of the 127 references it cites were found in a registry or an index.
Regulation of the NMDA Receptor Complex and Trafficking by Activity-Dependent Phosphorylation of the NR2B Subunit PDZ Ligand
Open accessAbstract
Interactions between NMDA receptors (NMDARs) and the PDZ [postsynaptic density-95 (PSD-95)/Discs large/zona occludens-1] domains of PSD-95/SAP90 (synapse-associated protein with a molecular weight of 90 kDa) family proteins play important roles in the synaptic targeting and signaling of NMDARs. However, little is known about the mechanisms that regulate these PDZ domain-mediated interactions. Here we show that casein kinase II (CK2) phosphorylates the serine residue (Ser1480) within the C-terminal PDZ ligand (IESDV) of the NR2B subunit of NMDAR in vitro and in vivo. Phosphorylation of Ser1480 disrupts the interaction of NR2B with the PDZ domains of PSD-95 and SAP102 and decreases surface NR2B expression in neurons. Interestingly, activity of the NMDAR and Ca 2+/calmodulin-dependent protein kinase II regulates CK2 phosphorylation of Ser1480. Furthermore, CK2 colocalizes with NR1 and PSD-95 at synaptic sites. These results indicate that activity-dependent CK2 phosphorylation of the NR2B PDZ ligand regulates the interaction of NMDAR with PSD-95/SAP90 family proteins as well as surface NMDAR expression and may be a critical mechanism for modulating excitatory synaptic function and plasticity.
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Diversity in NMDA Receptor Composition: Many Regulators, Many Consequences
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Metadata
- Authors
- Chung, H. J., Huang, Y. H., Lau, L.-F., & Huganir, R. L.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2004-11-10
- Volume
- 24
- Issue
- 45
- Pages
- 10248-10259
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W2096562774
- Cited by
- 313
- References
- 127
- FWCI
- 5.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Chung, H. J., Huang, Y. H., Lau, L.-F., & Huganir, R. L. (2004). Regulation of the NMDA Receptor Complex and Trafficking by Activity-Dependent Phosphorylation of the NR2B Subunit PDZ Ligand. The Journal of Neuroscience. https://doi.org/10.1523/jneurosci.0546-04.2004
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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