Yeast 1,3-β-Glucan Synthase Activity Is Inhibited by Phytosphingosine Localized to the Endoplasmic Reticulum

This publication has 45 references indexed in Scilit:

• Prenylation of Rho1p Is Required for Activation of Yeast 1,3-β-Glucan Synthase
  Published by Elsevier ,1999
• LST1 Is a SEC24 Homologue Used for Selective Export of the Plasma Membrane ATPase from the Endoplasmic Reticulum
  The Journal of cell biology, 1999
• Role of Lipid Modifications in Targeting Proteins to Detergent-resistant Membrane Rafts
  Journal of Biological Chemistry, 1999
• Involvement of Long Chain Fatty Acid Elongation in the Trafficking of Secretory Vesicles in Yeast
  The Journal of cell biology, 1998
• Activity of 1,3-β-D-Glucan Synthase Requires the GTP-binding Protein Rho1
  Journal of Biological Chemistry, 1996
• Identification of Yeast Rho1p GTPase as a Regulatory Subunit of 1,3-β-Glucan Synthase
  Science, 1996
• Rho1p, a Yeast Protein at the Interface Between Cell Polarization and Morphogenesis
  Science, 1996
• Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes.
  The Journal of cell biology, 1996
• Development of cell polarity in budding yeast
  Journal of Experimental Zoology, 1995
• Characterization and Gene Cloning of 1,3-beta-D-Glucan Synthase from Saccharomyces Cerevisiae
  European Journal of Biochemistry, 1995