Palmitoylation

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Overview

S-Palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine residues of membrane proteins.[1]

The precise function of palmitoylation depends on the particular protein being considered. Palmitoylation enhances the hydro-phobicity of proteins and contributes to their membrane association. Palmitoylation also appears to play a significant role in subcellular trafficking of proteins between membrane compartments, as well as in modulating protein-protein interactions.[2]

An example of a protein that undergoes palmitoylation is hemagglutinin, a membrane glycoprotein used by influenza to attach to host cell receptors. [3]

References

  1. Linder, M.E., "Reversible modification of proteins with thioester-linked fatty acids," Protein Lipidation, F. Tamanoi and D.S. Sigman, eds., pp. 215-40 (San Diego, CA: Academic Press, 2000).
  2. Basu, J., "Protein palmitoylation and dynamic modulation of protein function," Current Science, Vol. 87, No. 2, pp. 212-17 (25 July 2004).
  3. influenza viruses, the encyclopedia of virology, http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B7GG4-4CK7DHD-S&_rdoc=5&_hierId=42642&_refWorkId=141&_explode=42642&_alpha=I&_fmt=full&_orig=na&_docanchor=&_idxType=AR&view=c&_ct=10&_acct=C000011279&_version=1&_urlVersion=0&_userid=5399531&md5=607bbb1a7d18138457365550b9471eb5.