Palmitoylation and depalmitoylation dynamics at a glance.

@article{Conibear2010PalmitoylationAD,
  title={Palmitoylation and depalmitoylation dynamics at a glance.},
  author={Elizabeth Conibear and Nicholas G. Davis},
  journal={Journal of cell science},
  year={2010},
  volume={123 Pt 23},
  pages={4007-10}
}
Protein palmitoylation, the thioester linkage of fatty acyl moieties (typically, saturated 16C palmitate) to cysteine, is a lipid modification that serves both to tether proteins to membranes and to direct their localization to membrane microdomains. Unlike the two other types of lipid modification that also tether proteins to cytosolic membrane surfaces, namely prenylation and myristoylation, which remain attached to the protein throughout its lifetime, a distinguishing feature of… CONTINUE READING

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