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.

Abstract

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

Substances

  • 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