The yeast oxysterol binding protein Kes1 maintains sphingolipid levels

PLoS One. 2013 Apr 4;8(4):e60485. doi: 10.1371/journal.pone.0060485. Print 2013.

Abstract

The oxysterol binding protein family are amphitropic proteins that bind oxysterols, sterols, and possibly phosphoinositides, in a conserved binding pocket. The Saccharomyces cerevisiae oxysterol binding protein family member Kes1 (also known as Osh4) also binds phosphoinositides on a distinct surface of the protein from the conserved binding pocket. In this study, we determine that the oxysterol binding protein family member Kes1 is required to maintain the ratio of complex sphingolipids and levels of ceramide, sphingosine-phosphate and sphingosine. This inability to maintain normal sphingolipid homeostasis resulted in misdistribution of Pma1, a protein that requires normal sphingolipid synthesis to occur to partition into membrane rafts at the Golgi for its trafficking to the plasma membrane.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Cell Membrane / metabolism
  • Ceramides / metabolism
  • Golgi Apparatus / metabolism
  • Membrane Proteins / metabolism*
  • Protein Transport
  • Proton-Translocating ATPases / metabolism
  • Receptors, Steroid / metabolism*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sphingolipids / metabolism*

Substances

  • Ceramides
  • KES1 protein, S cerevisiae
  • Membrane Proteins
  • Receptors, Steroid
  • Saccharomyces cerevisiae Proteins
  • Sphingolipids
  • oxysterol binding protein
  • PMA1 protein, S cerevisiae
  • Proton-Translocating ATPases