Role of palmitoylation in RGS protein function

Methods Enzymol. 2004;389:33-55. doi: 10.1016/S0076-6879(04)89003-7.


Palmitoylation, the reversible, post-translational addition of palmitate to cysteine residues, occurs on several regulators of G-protein signaling (RGS) proteins. Palmitoylation can occur near the amino terminus, as for RGS4 and RGS16, but can also occur on a cysteine residue in the alpha4 helix of the RGS box, which is conserved in most RGS proteins. For some of the RGS proteins, palmitoylation is required to turn off G-protein signaling by accelerating GTP hydrolysis on the Galpha subunit. This article discusses the role of palmitoylation in RGS function and protocols are given for metabolic and in vitro labeling of RGS proteins with [3H]palmitate and measurement of GTP hydrolysis in membranes.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Membrane / chemistry
  • Cell Membrane / enzymology
  • Cell Membrane / metabolism
  • Conserved Sequence
  • Cysteine / metabolism
  • GTP Phosphohydrolases / metabolism
  • GTP-Binding Protein alpha Subunits, Gi-Go / metabolism
  • GTPase-Activating Proteins / metabolism
  • Guanosine Triphosphate / metabolism
  • Humans
  • Models, Molecular
  • Palmitic Acid / metabolism*
  • Protein Processing, Post-Translational
  • Protein Structure, Secondary
  • RGS Proteins / chemistry
  • RGS Proteins / genetics
  • RGS Proteins / metabolism*
  • Signal Transduction


  • GTPase-Activating Proteins
  • RGS Proteins
  • Palmitic Acid
  • Guanosine Triphosphate
  • GTP Phosphohydrolases
  • GTP-Binding Protein alpha Subunits, Gi-Go
  • Cysteine