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An unusual form of lipid linkage to the CD45 peptide

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Science  02 Nov 1990:
Vol. 250, Issue 4981, pp. 676-679
DOI: 10.1126/science.2146743

Abstract

Some protein kinases and phosphatases are myristoylated on their amino terminus, which perhaps contributes to subcellular localization or regulation. Glycoprotein CD45, a hematopoietic tyrosine phosphatase, was examined for fatty acid content. The CD45 protein incorporated [3H]myristate, but little [3H]palmitate. The label was not metabolized and reincorporated into amino acids or saccharides, as revealed by peptide maps of CD45 labeled with [3H]myristate, 14C-labeled amino acids, [35S]methionine, or 125I, and glycosidase treatments, respectively. The myristate label was resistant to mild alkaline methanolysis and was found in fatty acid and sphingosine, indicating an unusual form of lipid attachment to CD45.

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