Role of palmitoylation of postsynaptic proteins in promoting synaptic plasticity

Lucas Matt, Karam Kim, Dhrubajyoti Chowdhury, Johannes W Hell

Research output: Contribution to journalReview article

6 Scopus citations

Abstract

Many postsynaptic proteins undergo palmitoylation, the reversible attachment of the fatty acid palmitate to cysteine residues, which influences trafficking, localization, and protein interaction dynamics. Both palmitoylation by palmitoyl acyl transferases (PAT) and depalmitoylation by palmitoyl-protein thioesterases (PPT) is regulated in an activity-dependent, localized fashion. Recently, palmitoylation has received attention for its pivotal contribution to various forms of synaptic plasticity, the dynamic modulation of synaptic strength in response to neuronal activity. For instance, palmitoylation and depalmitoylation of the central postsynaptic scaffold protein postsynaptic density-95 (PSD-95) is important for synaptic plasticity. Here, we provide a comprehensive review of studies linking palmitoylation of postsynaptic proteins to synaptic plasticity.

Original languageEnglish (US)
Article number8
JournalFrontiers in Molecular Neuroscience
Volume12
DOIs
StatePublished - Feb 12 2019

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Keywords

  • AMPAR
  • Homeostatic plasticity
  • LTD
  • LTP
  • NMDAR
  • PSD-95

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience

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