| Literature DB >> 9576863 |
C Sütterlin1, M V Escribano, P Gerold, Y Maeda, M J Mazon, T Kinoshita, R T Schwarz, H Riezman.
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.Entities:
Mesh:
Substances:
Year: 1998 PMID: 9576863 PMCID: PMC1219463 DOI: 10.1042/bj3320153
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857