Efficient export of the glucose transporter Hxt1p from the endoplasmic reticulum requires Gsf2p

Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7415-20. doi: 10.1073/pnas.96.13.7415.

Abstract

Mutations in the GSF2 gene cause glucose starvation phenotypes in Saccharomyces cerevisiae. We have isolated the HXT1 gene, which encodes a low-affinity, high-capacity glucose transporter, as a multicopy suppressor of a gsf2 mutation. We show that gsf2 mutants accumulate Hxt1p in the endoplasmic reticulum (ER) and that Gsf2p is a 46-kDa integral membrane protein localized to the ER. gsf2 mutants also display a galactose growth defect and abnormal localization of the galactose transporter Gal2p but are not defective in function or localization of the high-affinity glucose transporter Hxt2p. These findings suggest that Gsf2p functions in the ER to promote the secretion of certain hexose transporters.

Publication types

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

MeSH terms

  • Biological Transport / genetics
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Gene Expression Regulation, Fungal*
  • Genes, Fungal
  • Glucose / metabolism*
  • Glucose Transport Proteins, Facilitative
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Monosaccharide Transport Proteins / genetics
  • Monosaccharide Transport Proteins / metabolism*
  • Mutation
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*

Substances

  • Fungal Proteins
  • Glucose Transport Proteins, Facilitative
  • Gsf2 protein, S cerevisiae
  • HXT1 protein, S cerevisiae
  • Membrane Proteins
  • Monosaccharide Transport Proteins
  • Saccharomyces cerevisiae Proteins
  • Glucose