Two classes of fatty acid acylated proteins exist in eukaryotic cells.

A. I. Magee, S. A. Courtneidge

Research output: Contribution to journalArticlepeer-review

89 Scopus citations


Labelling of cultured cells with [3H]palmitic and [3H]myristic acids demonstrates that each of these fatty acids modifies a substantially different subset of cellular proteins. Hydroxylamine treatment can be used to differentiate sensitive thioester linkages to palmitate from insensitive amide linkages to myristate. Several palmitoylated proteins are surface-oriented glycoproteins while all of the myristylated proteins appear to be internal. Myristate addition is much more tightly coupled to protein synthesis than palmitoylation, which is able to continue at a reduced level even in the prolonged absence of protein synthesis. Acyl proteins patterns were affected both qualitatively and quantitatively by transformation and growth status. The preferential addition of palmitate to the transferrin receptor and myristate to pp60src, and the absence of these modifications from several other proteins is reported. We propose a nomenclature for fatty acyl proteins based on these observations.

Original languageEnglish (US)
Pages (from-to)1137-1144
Number of pages8
JournalThe EMBO journal
Issue number5
StatePublished - May 1985
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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