English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Synaptic AMPA-type and NMDA-type glutamate receptors (AMPARs and NMDARs) have different dynamic characteristics critical for synaptic plasticity. We find that the posttranslational modification, palmitoylation, changes the conformation of postsynaptic density protein 95 (PSD95), a major synaptic scaffold, promoting interactions with AMPARs and NMDARs. In synapses, we measured the conformation and orientation of palmitoylated PSD95 relative to the scaffold, synapse-associated protein 97 (SAP97), and found that changing PSD95 palmitoylation altered PSD95 and AMPAR levels, but not NMDAR levels. We conclude that palmitoylation regulates PSD95 conformation and retention of AMPAR and NMDARs at synapses. Differences in PSD95 palmitoylation appear to occur when AMPARs and NMDARs are in separate synaptic domains, likely contributing to differences in AMPAR and NMDAR dynamics in synapses.

Palmitoylation regulates glutamate receptor distributions in postsynaptic densities through control of PSD95 conformation and orientation