Cited by 119Neuroscience and Neuropharmacology ResearchNicotinic Acetylcholine Receptors StudyReceptor Mechanisms and Signaling

The regulation of glutamate receptor trafficking and function by TARPs and other transmembrane auxiliary subunits

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Straub, Christoph, Tomita, Susumu·2012·Current Opinion in Neurobiology

Abstract

At excitatory synapses in the brain, glutamate released from nerve terminals binds to glutamate receptors to mediate signaling between neurons. Glutamate receptors expressed in heterologous cells show ion channel activity. Recently, native glutamate receptors were shown to contain auxiliary subunits that modulate the trafficking and/or channel properties. The AMPA receptor (AMPAR) can contain TARP and CNIHs as the auxiliary subunits, whereas kainate receptor (KAR) can contain the Neto auxiliary subunit. Each of these auxiliary subunits uniquely modulates the glutamate receptors, and determines properties of native glutamate receptors. A thorough elucidation of the properties of native glutamate receptor complexes is indispensable for the understanding of the molecular machinery that regulates glutamate receptors and excitatory synaptic transmission in the brain.

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Crossref · 10.1016/j.conb.2011.09.005

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  • AMPARs are decorated by auxiliary subunits that control their synthesis, trafficking, and biophysical properties.

    “Evidence has accumulated over the past decade indicating that AMPARs are not stand-alone receptors; rather, they are decorated by numerous types of auxiliary subunits that control the synthesis, trafficking, and biophysical properties of these receptors (278–281).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [280]

    The sections “Glutamate receptors and auxiliary subunits” and “Conclusions” say that AMPARs contain auxiliary subunits that regulate trafficking and channel properties. Our copy does not say that those subunits control AMPAR synthesis. (LLM, conf=0.88)

    Experimental — accuracy not yet measured
  • TARPs and CNIH2/3 regulate AMPAR channel properties and cellular and synaptic trafficking.

    “TARPs and CNIH2/3 regulate AMPAR channel properties and cellular and synaptic trafficking (Straub and Tomita, 2012, Maher et al., 2017, Jacobi and von Engelhardt, 2017).”

    From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Straub and Tomita, 2012

    The Conclusions state that TARPs modulate both AMPAR trafficking and channel properties, while CNIH2/3 modulate AMPAR channel properties. The section “Roles of CNIH2/3 in regulating AMPA receptors in the brain” reports enhanced AMPAR surface expression in heterologous cells but says whether CNIH2/3 promote trafficking in hippocampal neurons remains unresolved. Thus the claim overstates CNIH2/3’s established role in synaptic trafficking. (LLM, conf=0.86)

    Experimental — accuracy not yet measured
  • CNIH and TARPs likely compete for the same AMPAR binding sites, and one possible function of CNIH is to regulate the stoichiometry of TARP interaction, tuning the channel properties of associated AMPARs.

    “CNIH and TARPs likely compete for the same AMPAR binding sites (Straub and Tomita, 2012, Herring et al., 2013), and so one possible function of CNIH is to regulate the stoichiometry of TARP interaction, tuning the channel properties of the associated AMPARs.”

    From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Straub and Tomita, 2012

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Research works printed but not linked: 67

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Authors
Straub, C., & Tomita, S.
Affiliations
Yale University (US)
Corresponding author
Tomita, Susumu
Venue
Current Opinion in Neurobiology
Publisher
Elsevier BV
Published
2012-06
Volume
22
Issue
3
Pages
488-495
ISSN
0959-4388 (ISSN-L)
OpenAlex
W2021624177
Cited by
119
References
2
Citations by year
2024: 2 · 2023: 4 · 2022: 4 · 2021: 10 · 2020: 12 · 2019: 9 · 2018: 5 · 2017: 17 · 2016: 9 · 2015: 10 · 2014: 14 · 2013: 15 · 2012: 7
FWCI
1.13
Type
journal article
Language
en
Open access
Locations
  • Current Opinion in Neurobiology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
NIH (MH077939, MH085080)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
glutamate receptors, AMPA receptors, kainate receptors, TARP, auxiliary subunits, receptor trafficking, excitatory synaptic transmission, ion channel properties
MeSH terms
Animals, Models, Biological, Nuclear Proteins, Receptors, Glutamate, Protein Subunits, Protein Transport

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