Misregulation of phosphoinositides in Arabidopsis thaliana decreases pollen hydration and maternal fertility

Sex Plant Reprod. 2011 Dec;24(4):319-26. doi: 10.1007/s00497-011-0172-1. Epub 2011 Jun 21.


Phosphoinositides are important lipids involved in membrane identity, vesicle trafficking, and intracellular signaling. In recent years, phosphoinositides have been shown to play a critical role in polarized secretion in plants, as perturbations of phosphoinositide metabolism, through loss of function mutants, result in defects in root hair elongation and pollen tube growth, where polarized secretion occurs rapidly. In the Brassicaceae, responses of stigmatic papillae to compatible pollen are also thought to involve highly regulated secretory events to facilitate pollen hydration and penetration of the pollen tube through the stigmatic surface. We therefore sought to analyze the female sporophyte fertility of the root hair defective4-1 mutant and the PI 4-kinase β1/β2 double mutant, which differentially affect phosphatidylinositol-4-phosphate (PI4P) levels. Stigmas from both mutants supported slower rates of pollen grain hydration, and the fecundity of these mutants was also diminished as a result of failed pollination events. This study therefore concludes that PI4P is integral to appropriate pistil responses to compatible pollen.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-Phosphatidylinositol 4-Kinase / genetics
  • 1-Phosphatidylinositol 4-Kinase / metabolism
  • Arabidopsis / enzymology
  • Arabidopsis / genetics
  • Arabidopsis / growth & development
  • Arabidopsis / physiology*
  • Down-Regulation*
  • Phosphatidylinositols / metabolism*
  • Phosphoric Monoester Hydrolases / genetics
  • Phosphoric Monoester Hydrolases / metabolism
  • Pollen / enzymology
  • Pollen / genetics
  • Pollen / growth & development
  • Pollen / metabolism*
  • Reproduction
  • Water / metabolism*


  • Phosphatidylinositols
  • Water
  • 1-Phosphatidylinositol 4-Kinase
  • Phosphoric Monoester Hydrolases