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Dynamic extracellular interactions with AMPA receptors.

Hana Goldschmidt Merrion1, Casey N Barber1, Santosh Renuse2

  • 1Solomon H. Snyder Department of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, MD 21205.

Proceedings of the National Academy of Sciences of the United States of America
|November 17, 2025
PubMed
Summary

Researchers identified extracellular proteins interacting with AMPA receptors (AMPARs) during synaptic plasticity. These interactions, particularly with IgLON proteins like NTM, influence AMPAR surface mobility, impacting learning and memory.

Keywords:
AMPA receptorIgLONextracellularproximity proteomicssynaptic plasticity

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Synaptic plasticity is crucial for learning and memory in the central nervous system.
  • AMPA receptors (AMPARs) mediate fast synaptic transmission and their plasticity underlies memory formation.
  • The N-terminal domain (NTD) of AMPARs is implicated in synaptic targeting and plasticity, but its interactors are poorly understood.

Purpose of the Study:

  • To identify extracellular proteins interacting with AMPARs during synaptic plasticity.
  • To investigate the role of these interactors in regulating AMPAR function and synaptic plasticity.
  • To uncover novel mechanisms of extracellular regulation of AMPARs.

Main Methods:

  • Surface-restricted proximity labeling using APEX2-tagged AMPARs in cultured neurons.
  • Proteomics analysis (BioSITe) to identify differentially labeled proteins after chemical long-term potentiation.
  • Co-immunoprecipitation and overexpression studies to validate protein interactions and functional effects.

Main Results:

  • Identified 70 differentially labeled extracellular proteins associated with AMPARs during synaptic plasticity.
  • Discovered four IgLON family proteins (Ntm, OBCAM/Opcml, Negr1, Lsamp) as novel AMPAR interactors.
  • Demonstrated direct interaction of OBCAM and NTM with AMPAR extracellular domains.
  • Showed that NTM overexpression reduces surface AMPAR mobility in dendritic spines.

Conclusions:

  • The study reveals a dynamic extracellular interactome for AMPARs during synaptic plasticity.
  • IgLON proteins, particularly NTM, are key regulators of AMPAR surface dynamics and synaptic plasticity.
  • These findings provide insights into the unexplored extracellular regulation of AMPARs, with implications for synapse function, learning, and memory.