Fatty acylation of cellular proteins. Temporal and subcellular differences between palmitate and myristate acylation

E. N. Olson, G. Spizz

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

Previous studies demonstrated that palmitate and myristate are covalently linked to distinct sets of cellular proteins and that the linkages through which these fatty acids are attached to the polypeptide chains are different (Olson, E.N., Towler, D.A., and Glaser, L. (1985) J. Biol. Chem. 260, 3784-3790). In the present study, the kinetics and subcellular sites of acylation of proteins with palmitate and myristate were examined in the BC3H1 muscle cell line. Acylation with myristate was an extremely early modification that appeared to take place cotranslationally or shortly thereafter for a variety of soluble and membrane-bound proteins. In contrast, acylation of proteins with palmitate was a post-translational event that occurred exclusively on membrane proteins. To begin to understand the intracellular pathways that acyl proteins follow during their maturation, the degree of glycosylation, and the nature of the interaction of these proteins with membranes were examined. The majority of acyl proteins were tightly associated with mambranes and could not be removed by conditions that release peripheral proteins from membranes. However, only a minor fraction of acylated proteins were N-glycosylated. These data suggest that the acyltransferases that attach palmitate and myristate to proteins are present in different subcellular locations and demonstrate that these fatty acids are attached to newly synthesized acyl proteins at different times during their maturation. The lack of carbohydrate of the majority of integral membrane acyl proteins suggests that these proteins may follow intracellular pathways that are different from those followed by cell surface glycoproteins.

Original languageEnglish (US)
Pages (from-to)2458-2466
Number of pages9
JournalJournal of Biological Chemistry
Volume261
Issue number5
StatePublished - 1986

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Acylation
Palmitates
Myristic Acid
Membrane Proteins
Proteins
Fatty Acids
Membranes
Acyltransferases
Membrane Glycoproteins
Glycosylation
Muscle Cells
Carbohydrates
Muscle
Cell Line
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Fatty acylation of cellular proteins. Temporal and subcellular differences between palmitate and myristate acylation. / Olson, E. N.; Spizz, G.

In: Journal of Biological Chemistry, Vol. 261, No. 5, 1986, p. 2458-2466.

Research output: Contribution to journalArticle

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