We have demonstrated that more than 20 platelet proteins can be acylat
ed with fatty acids via thioester linkages. These include the glycopro
tein IX beta chain of glycoprotein Ib, components of the von Willebran
d factor receptor on the platelet surface, P-selectin, and alpha subun
its of G(z), G(q), and G(i). Our studies have shown that platelet prot
eins can be posttranslationally acylated in thioester linkages not onl
y with palmitate but with myristate and also with the eicosanoid precu
rsor fatty acids arachidonate and eicosapentaenoate. Thioesterificatio
n of platelet proteins with fatty acids other than palmitate may have
significant functional consequences for reversible binding of proteins
to membranes.