ArticleThe Journal of biological chemistry2014
The N-terminal domain modulates α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor desensitization.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Mapping the multi-domain allosteric network for CKAMP44 modulation of AMPA receptors.The Journal of biological chemistry · 2026Article
- GluA4 AMPA receptor gating mechanisms and modulation by auxiliary proteins.Nature structural & molecular biology · 2025Article
- Allosteric competition and inhibition in AMPA receptors.Nature structural & molecular biology · 2024Article
- Tuning synaptic strength by regulation of AMPA glutamate receptor localization.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024Review
- Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Review
- Distinct Cell Surface Expression Patterns of N-Glycosylation Site Mutants of AMPA-Type Glutamate Receptor under the Homo-Oligomeric Expression Conditions.International journal of molecular sciences · 2020Article
- Neto proteins regulate gating of the kainate-type glutamate receptor GluK2 through two binding sites.The Journal of biological chemistry · 2019Article
- Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM.Science (New York, N.Y.) · 2019Article
- Subunit-specific role for the amino-terminal domain of AMPA receptors in synaptic targeting.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Aggregation Limits Surface Expression of Homomeric GluA3 Receptors.The Journal of biological chemistry · 2016Article
- Probing Intersubunit Interfaces in AMPA-subtype Ionotropic Glutamate Receptors.Scientific reports · 2016Article
- Emerging structural insights into the function of ionotropic glutamate receptors.Trends in biochemical sciences · 2015Review
- Assembly of AMPA receptors: mechanisms and regulation.The Journal of physiology · 2015Review
- Mapping the interaction sites between AMPA receptors and TARPs reveals a role for the receptor N-terminal domain in channel gating.Cell reports · 2014Article
- Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states.Cell · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AMPA receptors are tetrameric glutamate-gated ion channels that mediate fast synaptic neurotransmission in mammalian brain. Their subunits contain a two-lobed N-terminal domain (NTD) that comprises over 40% of the mature polypeptide. The NTD is not obligatory for the assembly of tetrameric receptors, and its functional role is still unclear. By analyzing full-length and NTD-deleted GluA1-4 AMPA receptors expressed in HEK 293 cells, we found that the removal of the NTD leads to a significant reduction in receptor transport to the plasma membrane, a higher steady state-to-peak current ratio of glutamate responses, and strongly increased sensitivity to glutamate toxicity in cell culture. Further analyses showed that NTD-deleted receptors display both a slower onset of desensitization and a faster recovery from desensitization of agonist responses. Our results indicate that the NTD promotes the biosynthetic maturation of AMPA receptors and, for membrane-expressed channels, enhances the stability of the desensitized state. Moreover, these findings suggest that interactions of the NTD with extracellular/synaptic ligands may be able to fine-tune AMPA receptor-mediated responses, in analogy with the allosteric regulatory role demonstrated for the NTD of NMDA receptors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.