N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana

FEBS Lett. 2001 May 25;497(2-3):165-70. doi: 10.1016/s0014-5793(01)02453-x.


Phosphoinositide-specific phospholipase C's (PI-PLCs) are ubiquitous in eukaryotes, from plants to animals, and catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate into the two second messengers inositol 1,4,5-trisphosphate and diacylglycerol. In animals, four distinct subfamilies of PI-PLCs have been identified, and the three-dimensional structure of one rat isozyme, PLC-delta1, determined. Plants appear to contain only one gene family encoding PI-PLCs. The catalytic properties of plant PI-PLCs are very similar to those of animal enzymes. However, very little is known about the regulation of plant PI-PLCs. All plant PI-PLCs comprise three domains, X, Y and C2, which are also conserved in isoforms from animals and yeast. We here show that one PI-PLC isozyme from Arabidopsis thaliana, AtPLC2, is predominantly localized in the plasma membrane, and that the conserved N-terminal domain may represent an EF-hand domain that is required for catalytic activity but not for lipid binding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / enzymology*
  • Catalysis
  • Cell Membrane / enzymology
  • Conserved Sequence
  • Diglycerides / biosynthesis
  • EF Hand Motifs / physiology*
  • Inositol 1,4,5-Trisphosphate / biosynthesis
  • Isoenzymes / metabolism
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Phosphatidylinositol 4,5-Diphosphate / metabolism
  • Phosphatidylinositol Diacylglycerol-Lyase
  • Phosphoinositide Phospholipase C
  • Protein Structure, Tertiary / physiology
  • Sequence Deletion
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • Type C Phospholipases / metabolism*


  • Diglycerides
  • Isoenzymes
  • Phosphatidylinositol 4,5-Diphosphate
  • Inositol 1,4,5-Trisphosphate
  • Type C Phospholipases
  • Phosphoinositide Phospholipase C
  • Phosphatidylinositol Diacylglycerol-Lyase