Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/24168
Title: Saccharomyces cerevisiae GPI10, the functional homologue of human PIG-B, is required for glycosylphosphatidylinositol-anchor synthesis
Authors: Sütterlin, Christine, Escribano, M. Victoria, Mazón, María J., Riezman, Howard
Issue Date: 15-May-1998
Publisher: Biochemical Society
Abstract: An increasing number of plasma membrane proteins have been shown to be attached to the membrane via a glycosylphosphatidylinositol (GPI) moiety. All eukaryotes share a highly conserved GPI-core structure EthN-P-Man3-GlcN-PI, where EthN is ethanolamine. We have identified a protein encoded by the yeast open reading frame YGL142C that shares 33% identity with the human Pig-B protein. Deletion of this essential gene leads to a block in GPI anchor biosynthesis. We therefore named the gene GPI10. Gpi10p and Pig-B are functional homologues and the lethal deletion of GPI10 can be rescued by expression of the PIG-B cDNA. As found for PIG-B mutant cells, gpi10 deletant cells cannot attach the third mannose in an alpha-1,2 linkage to the GPI core-structure intermediate. Overexpression of GPI10 gives partial resistance to the GPI-synthesis inhibitor YW3548, suggesting that this gene product may affect the target of the inhibitor.
Description: 7 pages, 5 figures, 2 tables.-- et al.
Publisher version (URL): http://www.biochemj.org/bj/332/0153/bj3320153.htm
URI: http://hdl.handle.net/10261/24168
ISSN: 0264-6021
Citation: Biochemical Journal 332(1): 153-159 (1998)
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