A water-soluble analogue of glucosaminylphosphatidylinositol distinguishes two activities that palmitoylate inositol on GPI anchors

William T. Doerrler, Mark A. Lehrman

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

2-Palmitoylation of the inositol residue occurs during biosynthesis of glycosylphosphatidylinositol (GPI) anchors, but the enzymology of this step has been enigmatic. With endogenously synthesized glucosamine-PI (GlcN-PI; a GPI intermediate), a CoA-dependent palmitoyl-CoA-independent acyltransfer activity (AT-1) has been reported in rodent preparations. In contrast, a palmitoyl-CoA-dependent GlcN-PI acyltransferase activity (AT-2) was reported in both rodent and yeast preparations with a novel water-soluble dioctanoyl GlcN-PI analogue, GlcN-PI(C8). We report that AT-1, as well as AT-2, can be detected in rodent microsomes with GlcN-PI(C8), thus demonstrating the coexistence of these activities in a single membrane preparation and the general utility of GlcN-PI(C8) for studying the GPI pathway. Unexpectedly, AT-2 was peripherally associated with microsomes, a property atypical for GPI biosynthetic enzymes. (C) 200 Academic Press.

Original languageEnglish (US)
Pages (from-to)296-299
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume267
Issue number1
DOIs
StatePublished - Jan 7 2000

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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