Identification of N-terminal residues of Sonic Hedgehog important for palmitoylation by Hedgehog acyltransferase.

@article{Hardy2012IdentificationON,
  title={Identification of N-terminal residues of Sonic Hedgehog important for palmitoylation by Hedgehog acyltransferase.},
  author={Rayshonda Y Hardy and Marilyn D. Resh},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 51},
  pages={42881-9}
}
Sonic Hedgehog (Shh) is a secreted morphogen that regulates embryonic development. After removal of the signal peptide, Shh is processed to the mature, active form through autocleavage and a series of lipid modifications, including the attachment of palmitate. Covalent attachment of palmitate to the N-terminal cysteine of Shh is catalyzed by Hedgehog acyltransferase (Hhat) and is critical for proper signaling. The sequences within Shh that are responsible for palmitoylation by Hhat are not… CONTINUE READING