Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER

Andrew K. Sobering, Reika Watanabe, Martin J. Romeo, Benjamin C. Yan, Charles A. Specht, Peter Orlean, Howard Riezman, David E. Levin

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)637-648
Number of pages12
JournalCell
Volume117
Issue number5
DOIs
StatePublished - May 28 2004

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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