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AMPA receptor anchoring at CA1 synapses is determined by N-terminal domain and TARP γ8 interactions

Author

Listed:
  • Jake F. Watson

    (MRC Laboratory of Molecular Biology, Francis Crick Avenue
    IST Austria, Am Campus 1)

  • Alexandra Pinggera

    (MRC Laboratory of Molecular Biology, Francis Crick Avenue)

  • Hinze Ho

    (MRC Laboratory of Molecular Biology, Francis Crick Avenue
    University of Cambridge)

  • Ingo H. Greger

    (MRC Laboratory of Molecular Biology, Francis Crick Avenue)

Abstract

AMPA receptor (AMPAR) abundance and positioning at excitatory synapses regulates the strength of transmission. Changes in AMPAR localisation can enact synaptic plasticity, allowing long-term information storage, and is therefore tightly controlled. Multiple mechanisms regulating AMPAR synaptic anchoring have been described, but with limited coherence or comparison between reports, our understanding of this process is unclear. Here, combining synaptic recordings from mouse hippocampal slices and super-resolution imaging in dissociated cultures, we compare the contributions of three AMPAR interaction domains controlling transmission at hippocampal CA1 synapses. We show that the AMPAR C-termini play only a modulatory role, whereas the extracellular N-terminal domain (NTD) and PDZ interactions of the auxiliary subunit TARP γ8 are both crucial, and each is sufficient to maintain transmission. Our data support a model in which γ8 accumulates AMPARs at the postsynaptic density, where the NTD further tunes their positioning. This interplay between cytosolic (TARP γ8) and synaptic cleft (NTD) interactions provides versatility to regulate synaptic transmission and plasticity.

Suggested Citation

  • Jake F. Watson & Alexandra Pinggera & Hinze Ho & Ingo H. Greger, 2021. "AMPA receptor anchoring at CA1 synapses is determined by N-terminal domain and TARP γ8 interactions," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25281-4
    DOI: 10.1038/s41467-021-25281-4
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    Cited by:

    1. Nicky Scheefhals & Manon Westra & Harold D. MacGillavry, 2023. "mGluR5 is transiently confined in perisynaptic nanodomains to shape synaptic function," Nature Communications, Nature, vol. 14(1), pages 1-20, December.
    2. Martin Hruska & Rachel E. Cain & Matthew B. Dalva, 2022. "Nanoscale rules governing the organization of glutamate receptors in spine synapses are subunit specific," Nature Communications, Nature, vol. 13(1), pages 1-19, December.

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