Yeast Ras Regulates the Complex that Catalyzes the First Step in GPI-Anchor Biosynthesis at the ER

The yeast ERI1 gene encodes a small ER-localized protein that associates in vivo with GTP bound Ras2 in an effector loop-dependent manner. We showed previously that loss of Eri1 function results in hyperactive Ras phenotypes. Here, we demonstrate that Eri1 is a component of the GPI-GlcNAc transferas...

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Bibliographic Details
Published in:Cell 2004-05, Vol.117 (5), p.637-648
Main Authors: Sobering, Andrew K., Watanabe, Reika, Romeo, Martin J., Yan, Benjamin C., Specht, Charles A., Orlean, Peter, Riezman, Howard, Levin, David E.
Format: Article
Language:English
Subjects:
Carrier Proteins - genetics
Carrier Proteins - metabolism
Cell Wall - metabolism
Chitin - metabolism
Endoplasmic Reticulum - metabolism
Glycosylphosphatidylinositols - biosynthesis
Guanosine Triphosphate - metabolism
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mutation
ras Proteins - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Signal Transduction
Uridine Diphosphate N-Acetylglucosamine - metabolism
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Summary:The yeast ERI1 gene encodes a small ER-localized protein that associates in vivo with GTP bound Ras2 in an effector loop-dependent manner. We showed previously that loss of Eri1 function results in hyperactive Ras phenotypes. Here, we demonstrate that Eri1 is a component of the GPI-GlcNAc transferase (GPI-GnT) complex in the ER, which catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins. We also show that GTP bound Ras2 associates with the GPI-GnT complex in vivo and inhibits its activity, indicating that yeast Ras uses the ER as a signaling platform from which to negatively regulate the GPI-GnT. We propose that diminished GPI-anchor protein production contributes to hyperactive Ras phenotypes.
ISSN:0092-8674
1097-4172
DOI:10.1016/j.cell.2004.05.003