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J. Biol. Chem., Vol. 267, Issue 22, 15277-15280, Aug, 1992
AK Menon and VL Stevens
Numerous cell surface glycoproteins from eukaryotic organisms including
African trypanosomes and budding yeast (Saccharomyces cerevisiae), are
anchored to the lipid bilayer by a glycophospholipid,
glycosylphosphatidylinositol, covalently linked to the carboxyl terminus of
the protein via a phosphoethanolamine bridge. In this paper we describe
metabolic labeling experiments aimed at identifying the biosynthetic origin
of the ethanolamine residue in the phosphoethanolamine bridge. Using yeast
mutants generated by disruption of the ethanolaminephosphotransferase
(EPT1) and cholinephosphotransferase (CPT1) genes, we report data
consistent with the proposal that the ethanolamine residue is derived from
phosphatidylethanolamine.
Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein
Laboratory of Molecular Parasitology, Rockefeller University, New York, New York 10021.
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