dc.contributor.author |
Waites, CL |
en |
dc.contributor.author |
Specht, C |
en |
dc.contributor.author |
Hartel, K |
en |
dc.contributor.author |
Leal-Ortiz, S |
en |
dc.contributor.author |
Genoux, D |
en |
dc.contributor.author |
Li, Dong |
en |
dc.contributor.author |
Drisdel, RC |
en |
dc.contributor.author |
Jeyifous, O |
en |
dc.contributor.author |
Cheyne, JE |
en |
dc.contributor.author |
Green, WN |
en |
dc.contributor.author |
Montgomery, Johanna |
en |
dc.contributor.author |
Garner, CC |
en |
dc.date.accessioned |
2012-02-02T01:24:31Z |
en |
dc.date.issued |
2009 |
en |
dc.identifier.citation |
Journal of Neuroscience 29(14):4332-4345 2009 |
en |
dc.identifier.issn |
1529-2401 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/10861 |
en |
dc.description.abstract |
The synaptic insertion of GluR1-containing AMPA-type glutamate receptors (AMPARs) is critical for synaptic plasticity. However, mechanisms responsible for GluR1 insertion and retention at the synapse are unclear. The synapse-associated protein SAP97 directly binds GluR1 and participates in its forward trafficking from the Golgi network to the plasma membrane. Whether SAP97 also plays a role in scaffolding GluR1 at the postsynaptic membrane is controversial, attributable to its expression as a collection of alternatively spliced isoforms with ill-defined spatial and temporal distributions. In the present study, we have used live imaging and electrophysiology to demonstrate that two postsynaptic, N-terminal isoforms of SAP97 directly modulate the levels, dynamics, and function of synaptic GluR1-containing AMPARs. Specifically, the unique N-terminal domains confer distinct subsynaptic localizations onto SAP97, targeting the palmitoylated α-isoform to the postsynaptic density (PSD) and the L27 domain-containing β-isoform primarily to non-PSD, perisynaptic regions. Consequently, α- and βSAP97 differentially influence the subsynaptic localization and dynamics of AMPARs by creating binding sites for GluR1-containing receptors within their respective subdomains. These results indicate that N-terminal splicing of SAP97 can control synaptic strength by regulating the distribution of AMPARs and, hence, their responsiveness to presynaptically released glutamate. |
en |
dc.publisher |
Society for Neuroscience |
en |
dc.relation.ispartofseries |
Journal of Neuroscience |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/1529-2401/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.title |
Synaptic SAP97 isoforms regulate AMPA receptor dynamics and access to presynaptic glutamate |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1523/JNEUROSCI.4431-08.2009 |
en |
pubs.issue |
14 |
en |
pubs.begin-page |
4332 |
en |
pubs.volume |
29 |
en |
dc.rights.holder |
Copyright: Society for Neuroscience |
en |
dc.identifier.pmid |
19357261 |
en |
pubs.end-page |
4345 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
89688 |
en |
pubs.org-id |
Medical and Health Sciences |
en |
pubs.org-id |
Medical Sciences |
en |
pubs.org-id |
Physiology Division |
en |
pubs.record-created-at-source-date |
2010-09-01 |
en |
pubs.dimensions-id |
19357261 |
en |