Palmitoylation and localisation of RAS isoforms are modulated by the hypervariable linker domain.

@article{Laude2008PalmitoylationAL,
  title={Palmitoylation and localisation of RAS isoforms are modulated by the hypervariable linker domain.},
  author={Alex J Laude and Ian A Prior},
  journal={Journal of cell science},
  year={2008},
  volume={121 Pt 4},
  pages={421-7}
}
RAS isoforms have been proposed to exhibit differing biological outputs due to differences in their relative occupancy of cellular organelles and signalling microdomains. The membrane binding and targeting motifs of RAS are encoded by the C-terminal hypervariable region (HVR), and the precise localisation depends upon interactions between the HVR and the host membrane. Classic studies revealed that all RAS proteins rely on farnesylation and either palmitoylation or a polybasic stretch for… CONTINUE READING

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This motif comprises acidic residues that stabilise palmitoylation and basic amino acids that are likely to interact electrostatically with acidic phospholipids enriched at the cell surface .
This motif comprises acidic residues that stabilise palmitoylation and basic amino acids that are likely to interact electrostatically with acidic phospholipids enriched at the cell surface .
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