The Yeast Oxysterol Binding Protein Kes1 Maintains Sphingolipid Levels

Marissa A. LeBlanc, Gregory D. Fairn, Sarah B. Russo, Ola Czyz, Vanina Zaremberg, L. Ashley Cowart, Christopher R. McMaster

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

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.

Original languageEnglish
Article numbere60485
JournalPLoS One
Volume8
Issue number4
DOIs
Publication statusPublished - Apr 4 2013
Externally publishedYes

ASJC Scopus Subject Areas

  • General

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