Arv1 regulates PM and ER membrane structure and homeostasis but is dispensable for intracellular sterol transport. Academic Article uri icon

Overview

MeSH

  • Biological Transport, Active
  • Gene Deletion
  • Homeostasis
  • Lipid Metabolism

MeSH Major

  • Endoplasmic Reticulum
  • Ergosterol
  • Intracellular Membranes
  • Membrane Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins

abstract

  • The pan-eukaryotic endoplasmic reticulum (ER) membrane protein Arv1 has been suggested to play a role in intracellular sterol transport. We tested this proposal by comparing sterol traffic in wild-type and Arv1-deficient Saccharomyces cerevisiae. We used fluorescence microscopy to track the retrograde movement of exogenously supplied dehydroergosterol (DHE) from the plasma membrane (PM) to the ER and lipid droplets and high performance liquid chromatography to quantify, in parallel, the transport-coupled formation of DHE esters. Metabolic labeling and subcellular fractionation were used to assay anterograde transport of ergosterol from the ER to the PM. We report that sterol transport between the ER and PM is unaffected by Arv1 deficiency. Instead, our results indicate differences in ER morphology and the organization of the PM lipid bilayer between wild-type and arv1Δ cells suggesting a distinct role for Arv1 in membrane homeostasis. In arv1Δ cells, specific defects affecting single C-terminal transmembrane domain proteins suggest that Arv1 might regulate membrane insertion of tail-anchored proteins involved in membrane homoeostasis. © 2013 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.

publication date

  • August 2013

has subject area

  • Biological Transport, Active
  • Endoplasmic Reticulum
  • Ergosterol
  • Gene Deletion
  • Homeostasis
  • Intracellular Membranes
  • Lipid Metabolism
  • Membrane Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC3706471

Digital Object Identifier (DOI)

  • 10.1111/tra.12082

PubMed ID

  • 23668914

Additional Document Info

start page

  • 912

end page

  • 921

volume

  • 14

number

  • 8