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Raft localisation of FcgammaRIIa and efficient signaling are dependent on palmitoylation of cysteine 208.

Barnes NC, Powell MS, Trist HM, Gavin AL, Wines BD, Hogarth PM

  • Journal Immunology letters

  • Published 05 Dec 2005

  • Volume 104

  • ISSUE 1-2

  • Pagination 118-23

  • DOI 10.1016/j.imlet.2005.11.007


Ligand-dependent aggregation of FcgammaRIIa initiates multiple biochemical processes including the translocation to detergent resistant membrane domains (DRMs) and receptor tyrosine phosphorylation. Palmitoylation of cysteine residues is considered to be one process that assists in the localisation of proteins to DRMs. Within the juxtamembrane region of FcgammaRIIa there is cysteine residue (C208) that we show to be palmitoylated. Mutation of this cysteine residue results in the disruption of FcgammaRIIa translocation to DRMs as empirically defined by insolubility at high Triton X-100 concentrations. This study also demonstrates that the lack of lipid raft association diminishes FcgammaRIIa signaling as measured by receptor phosphorylation and calcium mobilisation functions suggesting that FcgammaRIIa signaling is partially dependent on lipid rafts.