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Cited by 73Neuroscience and Neuropharmacology ResearchGenetics and Neurodevelopmental DisordersAmino Acid Enzymes and Metabolism

AMPA Receptors in Synaptic Plasticity, Memory Function, and Brain Diseases

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de León-López, Cristina A. Muñoz, Carretero-Rey, Marta, Khan, Zafar U.·2025·Cellular and Molecular Neurobiology
DOI 10.1007/s10571-024-01529-7PMC PMC11754374
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Abstract

Tetrameric AMPA-type ionotropic glutamate receptors are primary transducers of fast excitatory synaptic transmission in the central nervous system, and their properties and abundance at the synaptic surface are crucial determinants of synaptic efficacy in neuronal communication across the brain. The induction of long-term potentiation (LTP) leads to the insertion of GluA1-containing AMPA receptors at the synaptic surface, whereas during long-term depression (LTD), these receptors are internalized into the cytoplasm of the spine. Disruptions in the trafficking of AMPA receptors to and from the synaptic surface attenuate both forms of synaptic plasticity. Homeostatic scaling up and scaling down, which are additional types of plasticity similar to LTP and LTD, are also regulated by the insertion and removal of GluA1-containing AMPA receptors from the synaptic surface. The trafficking of AMPA receptors is an intricate process assisted by various proteins. Furthermore, AMPA receptors are critical for the formation and consolidation of various types of memory, and alterations in their function are intimately associated with cognitive dysfunction in aging and several neurological and psychiatric diseases. In this review, we will provide an overview of the current understanding of how AMPA receptors regulate various forms of synaptic plasticity, their contribution to memory functions, and their role in aging and brain diseases.

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  • LTD involves dissociation of GluA1 subunits from the GluA1-TARP-(PSD-95) complex, followed by dephosphorylation of TARP by PP1 and dephosphorylation of GluA1 at S845, which collectively promote receptor endocytosis.

    “This process involves the dissociation of GluA1 subunits from the GluA1-TARP-(PSD-95) complex, followed by dephosphorylation of TARP by protein phosphatase 1 (PP1) and dephosphorylation of GluA1 at the S845 site, which collectively promote receptor endocytosis [45].”

    From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [45]

    The “GluA1-Containing AMPA Receptors in LTD” section supports the roles of PP1-mediated TARP dephosphorylation and GluA1 S845 dephosphorylation in receptor endocytosis. It does not support the claimed order: it says PP1 dephosphorylation disrupts the TARP–PSD-95 interaction, leading to GluA1 release, rather than following dissociation. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

  • Phosphorylation of GluA1 at S831 and TARPs enhances AMPAR single-channel conductance.

    “This phosphorylation enhances AMPAR single-channel conductance and promotes their trapping at the synaptic surface, leading to synaptic strengthening [45].”

    From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [45]

    In “AMPA Receptors in Hebbian Forms of Plasticity,” the paper states that GluA1 S831 phosphorylation increases single-channel conductance. The same section says TARP phosphorylation facilitates trapping of GluA1-containing AMPA receptors at the synaptic surface, but does not say that TARP phosphorylation increases single-channel conductance. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • The precise number, subtype, and localization of glutamate receptors at the postsynaptic membrane are dynamically regulated through complex trafficking mechanisms, which are crucial for synaptic plasticity and cognitive functions like learning and memory.

    “The precise number, subtype, and localization of glutamate receptors at the postsynaptic membrane are dynamically regulated through complex trafficking mechanisms, which are crucial for synaptic plasticity and cognitive functions like learning and memory [45].”

    From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [45]

    Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.

    Experimental — accuracy not yet measured

  • CaMKII activated by calcium influx during LTP phosphorylates GluA1 at the S831 site and TARPs at S277 and S281 sites.

    “Thus, CaMKII, activated by calcium influx during LTP, phosphorylates GluA1 at the S831 site and TARPs at S277 and S281 sites.”

    From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [45]

    The ‘AMPA Receptors in Hebbian Forms of Plasticity’ section says LTP-induced calcium influx activates CaMKII, which phosphorylates GluA1 at S831 and auxiliary proteins including TARPs. It identifies S277 and S281 specifically as sites on TARPγ8, so the claim is broader than the source if ‘TARPs’ means the family generally. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • LTD is calcium-dependent, but typically involves a smaller or more prolonged calcium influx compared to LTP.

    “Similar to LTP, LTD is also calcium-dependent, but typically involves a smaller or more prolonged calcium influx compared to LTP.”

    From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [45]

    In the ‘Ca2+-Permeable AMPA Receptors in LTP and LTD’ subsection (page not provided), the paper says a calcium-dependent phosphatase is essential for receptor endocytosis during LTD, supporting calcium involvement. It does not say that LTD typically involves a smaller or more prolonged calcium influx than LTP. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

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Authors
de León-López, C. A. M., Carretero-Rey, M., & Khan, Z. U.
Affiliations
Instituto de Salud Carlos III (ES)
Corresponding author
Khan, Zafar U.
ORCID
Khan, Zafar U.
Venue
Cellular and Molecular Neurobiology
Publisher
Springer Science and Business Media LLC
Published
2025-01-22
Volume
45
Issue
1
Pages
14-14
ISSN
  • 0272-4340 (ISSN-L)
  • 1573-6830
DOI
10.1007/s10571-024-01529-7
PMC
PMC11754374
OpenAlex
W4406726334
Cited by
73
References
186
Citations by year
2026: 49 · 2025: 24
FWCI
8.80
Type
journal article
Language
en
Open access
Licence
Locations
  • Cellular and Molecular Neurobiology (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Repositorio Institucional de la Universidad de Málaga (University of Málaga) (submittedVersion, cc-by)
Funders
  • Ministerio de Ciencia, Innovación y Universidades, Spain (PID2022-136954OB-I00)
  • Junta de Andalucía, Spain (PROYEXCEL-00422)
  • Fondo Europeo de Desarrollo Regional , EU (CTS-586-G-FEDER)
  • Universidad de Málaga
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Keywords
AMPA receptors, GluR1, synaptic plasticity, long-term potentiation, long-term depression, homeostatic synaptic scaling, receptor trafficking, synaptic homeostasis, memory formation, memory consolidation, cognitive aging, neurological disorders, mental illness, ionotropic glutamate receptors
MeSH terms
Animals, Brain Diseases, Humans, Memory, Neuronal Plasticity, Synapses, Receptors, AMPA

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