P-selectin is acylated with palmitic acid and stearic acid at cysteine 766 through a thioester linkage

T. Fujimoto, E. Stroud, R. E. Whatley, S. M. Prescott, L. Muszbek, M. Laposata, R. P. McEver

Research output: Contribution to journalArticle

45 Scopus citations

Abstract

We report that the adhesion receptor P-selectin can be metabolically labeled with [3H]palmitic acid in human platelets. Analysis of alkaline methanolysis products from labeled protein demonstrated that the radioactivity associated with P-selectin was covalently bound palmitic acid. [3H]Palmitic acid was cleaved by hydroxylamine treatment at neutral pH and by reducing agents, indicating that acylation occurred through a thioester linkage. Both stearic acid and palmitic acid were detected by gas chromatography-mass spectrometry analysis of alkaline hydrolysates of purified P-selectin. Deletion or mutation of Cys766 eliminated [3H]palmitic acid labeling of P-selectin in transfected COS-7 cells. We conclude that the cytoplasmic domain of P-selectin is acylated at Cys766 through a thioester bond. Fatty acid acylation may regulate intracellular trafficking or other functions of P-selectin.

Original languageEnglish (US)
Pages (from-to)11394-11400
Number of pages7
JournalJournal of Biological Chemistry
Volume268
Issue number15
StatePublished - 1993

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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