Ca2+/calmodulin binding to PSD-95 downregulates its palmitoylation and ampars in long-term depression

Dhrubajyoti Chowdhury, Johannes W. Hell

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


AMPA-type glutamate receptors (AMPARs) are clustered into functional nanodomains at postsynaptic sites through anchorage by the scaffolding protein, postsynaptic density protein-95 (PSD-95). The synaptic abundance of AMPARs is dynamically controlled in various forms of synaptic plasticity. Removal of AMPARs from the synapse in long-term depression (LTD) requires mobilization of PSD-95 away from the synapse. The molecular mechanisms underlying PSD-95 dispersal from the synapse during LTD are not completely understood. Here we show that, following Ca2+ influx, binding of Ca2+/calmodulin (CaM) to PSD-95 triggers loss of synaptic PSD-95 as well as surface AMPARs during chemically induced LTD in cultured rat neurons. Our data suggest that a reduction in PSD-95 palmitoylation mediates the effect of Ca2+/CaM on PSD-95 synaptic levels during LTD. These findings reveal a novel molecular mechanism for synaptic AMPAR regulation in LTD.

Original languageEnglish (US)
Article number6
Pages (from-to)1-10
Number of pages10
JournalFrontiers in Synaptic Neuroscience
StatePublished - 2019


  • LTD
  • Palmitoylation
  • PSD-95
  • Synapse

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Cell Biology


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