ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2014
Molecular dissection of the interaction between the AMPA receptor and cornichon homolog-3.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.
- Evidence of CNIH3 involvement in opioid dependence.Molecular psychiatry · 2016Pooled it
- The AMPA receptor life cycle: assembly, regulation and synaptic diversity.Nature reviews. Neuroscience · 2026Review
- Trafficking of the human NaProtein science : a publication of the Protein Society · 2026Article
- LDHA, BIK, and CNIH4 Are Diagnostic Markers of Endoplasmic Reticulum Stress in Lung Cancer Comorbid With Sepsis: Integrating Machine Learning and Single-Cell Analysis of Immune Signaling.Mediators of inflammation · 2026Article
- Integrated multi-omic characterizations of the synapse reveal RNA processing factors and ubiquitin ligases associated with neurodevelopmental disorders.Cell systems · 2025Article
- The Role of Cornichons in the Biogenesis and Functioning of Monovalent-Cation Transport Systems.Physiological research · 2024Review
- Transcriptomic profile of premature ovarian insufficiency with RNA-sequencing.Frontiers in cell and developmental biology · 2024Article
- Comprehensive analysis of clinical prognosis and biological significance of CNIH4 in cervical cancer.Cancer medicine · 2023Article
- Article
- The electroretinogram b-wave amplitude: a differential physiological measure for Attention Deficit Hyperactivity Disorder and Autism Spectrum Disorder.Journal of neurodevelopmental disorders · 2022Article
- Sex Differences in the Role of CNIH3 on Spatial Memory and Synaptic Plasticity.Biological psychiatry · 2021Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Article
- CaThe Journal of physiology · 2021Article
- Proteomic insights into synaptic signaling in the brain: the past, present and future.Molecular brain · 2021Review
- Genome-Wide Association Analysis of Neonatal White Matter Microstructure.Cerebral cortex (New York, N.Y. : 1991) · 2021Article
- AMPA receptor structure and auxiliary subunits.The Journal of physiology · 2021Review
- Structures of the AMPA receptor in complex with its auxiliary subunit cornichon.Science (New York, N.Y.) · 2019Article
- AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking.Cellular and molecular life sciences : CMLS · 2019Review
- Engineering defined membrane-embedded elements of AMPA receptor induces opposing gating modulation by cornichon 3 and stargazin.The Journal of physiology · 2017Article
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 4 countries.
Funding
Abstract
Cornichon homologs (CNIHs) are AMPA-type glutamate receptor (AMPAR) auxiliary subunits that modulate AMPAR ion channel function and trafficking. Mechanisms underlying this interaction and functional modulation of the receptor complex are currently unclear. Here, using proteins expressed from mouse and rat cDNA, we show that CNIH-3 forms a stable complex with tetrameric AMPARs and contributes to the transmembrane density in single-particle electron microscopy structures. Peptide array-based screening and in vitro mutagenesis identified two clusters of conserved membrane-proximal residues in CNIHs that contribute to AMPAR binding. Because CNIH-1 binds to AMPARs but modulates gating at a significantly lower magnitude compared with CNIH-3, these conserved residues mediate a direct interaction between AMPARs and CNIHs. In addition, residues in the extracellular loop of CNIH-2/3 absent in CNIH-1/4 are critical for both AMPAR interaction and gating modulation. On the AMPAR extracellular domains, the ligand-binding domain and possibly a stretch of linker, connecting the ligand-binding domain to the fourth membrane-spanning segment, is the principal contact point with the CNIH-3 extracellular loop. In contrast, the membrane-distal N-terminal domain is less involved in AMPAR gating modulation by CNIH-3 and AMPAR binding to CNIH-3. Collectively, our results identify conserved residues in the membrane-proximal region of CNIHs that contribute to AMPAR binding and an additional unique segment in the CNIH-2/3 extracellular loop required for both physical interaction and gating modulation of the AMPAR. Consistent with the dissociable properties of binding and gating modulation, we identified a mutant CNIH-3 that preserves AMPAR binding capability but has attenuated activity of gating modulation.
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Registered trials
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.