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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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 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.[1]

References

  1. Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER. Sobering, A.K., Watanabe, R., Romeo, M.J., Yan, B.C., Specht, C.A., Orlean, P., Riezman, H., Levin, D.E. Cell (2004) [Pubmed]
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