P-selectin is acylated with palmitic acid and stearic acid at cysteine 766 through a thioester linkage.
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Fujimoto T, Stroud E, Whatley RE, Prescott SM, Muszbek L, Laposata M, McEver RP
P-selectin is acylated with palmitic acid and stearic acid at cysteine 766 through a thioester linkage.
J Biol Chem. 1993 May 25;268(15):11394-400.
- PubMed ID
- 7684381 [ View in PubMed]
- 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.