Phospholipase D as an effector for ADP-ribosylation factor in the regulation of vesicular traffic

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

Research output: Contribution to journalArticle

49 Scopus citations

Abstract

A mammalian phospholipase D (PLD) activity that is stimulated by ADP-ribosylation factor (ARF) has been identified in Golgi-enriched membrane fractions. This activity is due to the PLD1 isoform and evidence from several laboratories indicates that PLD1 is important for the polymerization of vesicle coat proteins on membranes. When expressed in Chinese hamster ovary cells, PLD1 localized to dispersed small vesicles that overlapped with the location of the ERGIC53 protein, a marker for the endoplasmic reticulum (ER)-Golgi intermediate compartment. Cells having increased PLD1 expression had accelerated anterograde and retrograde transport between the ER and Golgi. Membranes from cells having elevated PLD 1 activity bound more COPI, ARF, and ARF-GTPase activating protein. These membranes also produced more COPI vesicles than did membranes from control cells. It is likely that PLD1 participates in both positive and negative feedback regulation of the formation of COPI vesicles and is important for controlling the rate of this process. Copyright (C) 1999 Elsevier Science Ireland Ltd.

Original languageEnglish (US)
Pages (from-to)141-152
Number of pages12
JournalChemistry and Physics of Lipids
Volume98
Issue number1-2
DOIs
StatePublished - Apr 1 1999

Keywords

  • ADP-ribosylation factor
  • Diacylglycerol
  • Phosphatidic acid
  • Phosphatidylinositol (4,5)bisphosphate
  • Phospholipase D
  • Vesicle transport

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Cell Biology

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