Phosphatidic acid formation by phospholipase D is required for transport from the endoplasmic reticulum to the Golgi complex

Kun Bi, Michael G. Roth, Nicholas T. Ktistakis

Research output: Contribution to journalArticle

152 Scopus citations

Abstract

Background: Lipid molecules may play a regulatory role in the secretory pathway of mammals and yeast. The lipid hydrolase phospholipase D (PLD) is one candidate for mediating regulation of secretion, based on the location of this enzyme and its requirements for activation. Results: We found that primary alcohols, which block formation of phosphatidic acid (PA) by PLD, inhibited the transport of two different viral glycoproteins from the endoplasmic reticulum to the Golgi complex in Chinese hamster ovary cells. Corresponding secondary alcohols, which are much less potent in blocking PA formation, were also less effective in blocking transport of the glycoproteins. The block in glycoprotein transport imposed by primary alcohols was reversed when PA, in the form of liposomes, was exogenously supplied to the culture medium. Conclusions: We suggest that the earliest site of regulation of membrane transport by PLD is within the intermediate compartment between the endoplasmic reticulum and the Golgi complex.

Original languageEnglish (US)
Pages (from-to)301-307
Number of pages7
JournalCurrent Biology
Volume7
Issue number5
DOIs
StatePublished - May 1 1997

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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