Requirement of Phosphoinositides Containing Stearic Acid To Control Cell Polarity

Mol Cell Biol. 2016 Feb 16;36(5):765-80. doi: 10.1128/MCB.00843-15. Epub 2015 Dec 28.

Abstract

Phosphoinositides (PIPs) are present in very small amounts but are essential for cell signaling, morphogenesis, and polarity. By mass spectrometry, we demonstrated that some PIPs with stearic acyl chains were strongly disturbed in a psi1Δ Saccharomyces cerevisiae yeast strain deficient in the specific incorporation of a stearoyl chain at the sn-1 position of phosphatidylinositol. The absence of PIPs containing stearic acid induced disturbances in intracellular trafficking, although the total amount of PIPs was not diminished. Changes in PIPs also induced alterations in the budding pattern and defects in actin cytoskeleton organization (cables and patches). Moreover, when the PSI1 gene was impaired, a high proportion of cells with bipolar cortical actin patches that occurred concomitantly with the bipolar localization of Cdc42p was specifically found among diploid cells. This bipolar cortical actin phenotype, never previously described, was also detected in a bud9Δ/bud9Δ strain. Very interestingly, overexpression of PSI1 reversed this phenotype.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Actins / ultrastructure
  • Acyltransferases / genetics
  • Acyltransferases / metabolism
  • Cell Polarity
  • Gene Deletion
  • Phosphatidylinositols / chemistry
  • Phosphatidylinositols / genetics
  • Phosphatidylinositols / metabolism*
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Stearic Acids / analysis
  • Stearic Acids / metabolism*

Substances

  • Actins
  • Phosphatidylinositols
  • Saccharomyces cerevisiae Proteins
  • Stearic Acids
  • stearic acid
  • Acyltransferases
  • Cst26 protein, S cerevisiae

Grants and funding

This work was supported by CNRS and Université de Bordeaux.