"Slip, sliding away": phospholipase D and the Golgi apparatus

Trends Cell Biol. 2003 Oct;13(10):540-6. doi: 10.1016/j.tcb.2003.08.004.

Abstract

Phospholipase D enzymes (PLDs) constitute a family of phosphodiesterases that catalyze the hydrolysis of phosphatidylcholine (PtdCho) to generate choline and phosphatidic acid (PtdOH), a potent lipid signaling molecule implicated in numerous physiological processes. Mammalian PLDs have been localized to multiple organelles, including the nucleus, Golgi apparatus, lysosomes, secretory granules and plasma membrane. However, the detailed mechanisms that govern targeting of PLDs to different organelles, how their local activity is controlled or indeed the nature of PA effectors are not well understood. Here, we discuss recent observations on PLD localization to the Golgi apparatus and how members of this enzyme family might play a role in regulating the structure of this organelle.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Golgi Apparatus / enzymology*
  • Phosphatidic Acids / metabolism
  • Phosphatidylinositols / biosynthesis
  • Phospholipase D / chemistry
  • Phospholipase D / metabolism*
  • Research Design

Substances

  • Phosphatidic Acids
  • Phosphatidylinositols
  • Phospholipase D