Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins

Biochim Biophys Acta. 1999 Aug 12;1451(1):1-16. doi: 10.1016/s0167-4889(99)00075-0.


Covalent attachment of myristate and/or palmitate occurs on a wide variety of viral and cellular proteins. This review will highlight the latest advances in our understanding of the enzymology of N-myristoylation and palmitoylation as well as the functional consequences of fatty acylation of key signaling proteins. The role of myristate and palmitate in promoting membrane binding as well as specific membrane targeting will be reviewed, with emphasis on the Src family of tyrosine protein kinases and alpha subunits of heterotrimeric G proteins. The use of myristoyl switches and regulated depalmitoylation as mechanisms for achieving reversible membrane binding and regulated signaling will also be explored.

Publication types

  • Review

MeSH terms

  • Acylation
  • Acyltransferases / chemistry*
  • Amino Acid Sequence
  • Cell Membrane / chemistry
  • Molecular Sequence Data
  • Myristic Acid / chemistry
  • Palmitic Acid / chemistry
  • Protein Binding
  • Protein Sorting Signals / chemistry*
  • Proteins / chemistry*


  • Protein Sorting Signals
  • Proteins
  • Myristic Acid
  • Palmitic Acid
  • Acyltransferases
  • G-protein palmitoyltransferase
  • glycylpeptide N-tetradecanoyltransferase