Role of palmitoylation of postsynaptic proteins in promoting synaptic plasticity

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

Research output: Contribution to journalReview articlepeer-review

27 Scopus citations


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
StatePublished - Feb 12 2019
Externally publishedYes


  • Homeostatic plasticity
  • LTD
  • LTP
  • PSD-95

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience


Dive into the research topics of 'Role of palmitoylation of postsynaptic proteins in promoting synaptic plasticity'. Together they form a unique fingerprint.

Cite this