Protein kinase C and phospholipase D: intimate interactions in intracellular signaling

Cell Mol Life Sci. 2005 Jul;62(13):1448-61. doi: 10.1007/s00018-005-4531-7.

Abstract

Diacylglycerol (DAG) was discovered as a potent lipid second messenger with protein kinase C (PKC) as its major cellular target more than 25 years ago. There is increasing evidence of significant complexity within lipid signaling, and the classical DAG-PKC model no longer stands alone but is part of a larger bioactive lipid universe involving glycerolipids and sphingolipids. Multiple layers of regulation exist among PKC- and DAG-metabolizing enzymes such as phosphatidylcholine (PC)-specific phospholipase D, and cross-talk exists between the glycerolipid and sphingolipid pathways, with PKC at the center. Currently, there is intense interest in the question of whether DAG derived from PC can function as a lipid second messenger and regulate PKC analogous to DAG derived from phosphatidylinositol-4,5-bisphosphate (PIP2). To address these issues and incorporate DAG-PKC and other signaling pathways into an expanded view of cell biology, it will be necessary to go beyond the classical approaches and concepts.

Publication types

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

MeSH terms

  • Animals
  • Ceramides / metabolism
  • Diglycerides / metabolism*
  • Humans
  • Phosphatidic Acids / metabolism
  • Phospholipase D / metabolism*
  • Protein Kinase C / metabolism*
  • Signal Transduction*

Substances

  • Ceramides
  • Diglycerides
  • Phosphatidic Acids
  • Protein Kinase C
  • Phospholipase D