Phosphatidyl ethanolamine is essential for targeting the arginine transporter Can1p to the plasma membrane of yeast

Biochim Biophys Acta. 2002 Aug 19;1564(1):9-13. doi: 10.1016/s0005-2736(02)00455-8.


In continuation of our previous study, we show that phosphatidyl ethanolamine (PE) depletion affects, in addition to amino acid transporters, activities of at least two other proton motive force (pmf)-driven transporters (Ura4p and Mal6p). For Can1p, we demonstrate that the lack of PE results in a failure of the permease targeting to plasma membrane. Despite the pleiotropic effect of PE depletion, a specific role of PE in secretion of a defined group of permeases can be distinguished. Pmf-driven transporters are more sensitive to the lack of PE than other plasma membrane proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Transport Systems / genetics
  • Amino Acid Transport Systems / metabolism*
  • Amino Acid Transport Systems, Basic
  • Arginine / metabolism*
  • Cell Membrane / metabolism
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Glucose Transport Proteins, Facilitative
  • Mannosyltransferases
  • Membrane Proteins / metabolism
  • Monosaccharide Transport Proteins / metabolism
  • Phosphatidylethanolamines / metabolism*
  • Proton-Motive Force
  • Proton-Translocating ATPases / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Schizosaccharomyces pombe Proteins*
  • Vesicular Transport Proteins


  • Amino Acid Transport Systems
  • Amino Acid Transport Systems, Basic
  • CAN1 protein, Candida albicans
  • Fungal Proteins
  • Glucose Transport Proteins, Facilitative
  • HXT1 protein, S cerevisiae
  • Membrane Proteins
  • Monosaccharide Transport Proteins
  • Phosphatidylethanolamines
  • SHR3 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins
  • Vesicular Transport Proteins
  • ura4 protein, S pombe
  • arginine permease
  • Arginine
  • ANP1 protein, S cerevisiae
  • Mannosyltransferases
  • PMA1 protein, S cerevisiae
  • Proton-Translocating ATPases