---
_id: '9985'
abstract:
- lang: eng
text: 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.
acknowledgement: The authors are very grateful to Andrew Penn for advice and discussions
on surface receptor labelling in slice tissue, dissociated culture transfection,
and for providing tdTomato and BirAER expression plasmids. This work would not have
been possible without support from the Biological Services teams at both the Laboratory
of Molecular Biology and Ares facilities. We are also very grateful to Nick Barry
and Jerome Boulanger of the LMB Light Microscopy facility for support with confocal
and STORM imaging and analysis, Junichi Takagi for providing scFv-Clasp expression
constructs, Veronica Chang for assistance with scFv-Clasp protein production, and
Nejc Kejzar for assistance with cluster analysis. We would like to thank Teru Nakagawa
and Ole Paulsen for critical reading of the manuscript and constructive feedback.
This work was supported by grants from the Medical Research Council (MC_U105174197)
and BBSRC (BB/N002113/1).
article_number: '5083'
article_processing_charge: Yes
article_type: original
author:
- first_name: Jake
full_name: Watson, Jake
id: 63836096-4690-11EA-BD4E-32803DDC885E
last_name: Watson
orcid: 0000-0002-8698-3823
- first_name: Alexandra
full_name: Pinggera, Alexandra
last_name: Pinggera
- first_name: Hinze
full_name: Ho, Hinze
last_name: Ho
- first_name: Ingo H.
full_name: Greger, Ingo H.
last_name: Greger
citation:
ama: Watson J, Pinggera A, Ho H, Greger IH. AMPA receptor anchoring at CA1 synapses
is determined by N-terminal domain and TARP γ8 interactions. Nature Communications.
2021;12(1). doi:10.1038/s41467-021-25281-4
apa: Watson, J., Pinggera, A., Ho, H., & Greger, I. H. (2021). AMPA receptor
anchoring at CA1 synapses is determined by N-terminal domain and TARP γ8 interactions.
Nature Communications. Nature Publishing Group. https://doi.org/10.1038/s41467-021-25281-4
chicago: Watson, Jake, Alexandra Pinggera, Hinze Ho, and Ingo H. Greger. “AMPA Receptor
Anchoring at CA1 Synapses Is Determined by N-Terminal Domain and TARP Γ8 Interactions.”
Nature Communications. Nature Publishing Group, 2021. https://doi.org/10.1038/s41467-021-25281-4.
ieee: J. Watson, A. Pinggera, H. Ho, and I. H. Greger, “AMPA receptor anchoring
at CA1 synapses is determined by N-terminal domain and TARP γ8 interactions,”
Nature Communications, vol. 12, no. 1. Nature Publishing Group, 2021.
ista: Watson J, Pinggera A, Ho H, Greger IH. 2021. AMPA receptor anchoring at CA1
synapses is determined by N-terminal domain and TARP γ8 interactions. Nature Communications.
12(1), 5083.
mla: Watson, Jake, et al. “AMPA Receptor Anchoring at CA1 Synapses Is Determined
by N-Terminal Domain and TARP Γ8 Interactions.” Nature Communications,
vol. 12, no. 1, 5083, Nature Publishing Group, 2021, doi:10.1038/s41467-021-25281-4.
short: J. Watson, A. Pinggera, H. Ho, I.H. Greger, Nature Communications 12 (2021).
date_created: 2021-09-05T22:01:23Z
date_published: 2021-08-23T00:00:00Z
date_updated: 2023-08-11T11:07:51Z
day: '23'
ddc:
- '612'
department:
- _id: PeJo
doi: 10.1038/s41467-021-25281-4
external_id:
isi:
- '000687672000006'
pmid:
- '34426577 '
file:
- access_level: open_access
checksum: 1bf4f6a561f96bc426d754de9cb57710
content_type: application/pdf
creator: cchlebak
date_created: 2021-09-08T12:57:06Z
date_updated: 2021-09-08T12:57:06Z
file_id: '9991'
file_name: 2021_NatureCommunications_Watson.pdf
file_size: 18310502
relation: main_file
success: 1
file_date_updated: 2021-09-08T12:57:06Z
has_accepted_license: '1'
intvolume: ' 12'
isi: 1
issue: '1'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
eissn:
- 2041-1723
publication_status: published
publisher: Nature Publishing Group
quality_controlled: '1'
scopus_import: '1'
status: public
title: AMPA receptor anchoring at CA1 synapses is determined by N-terminal domain
and TARP γ8 interactions
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 12
year: '2021'
...