Benghezal M, et al. (1996) Yeast Gpi8p is essential for GPI anchor attachment onto proteins. EMBO J 15(23):6575-83
Abstract: Glycosylphosphatidylinositol (GPI) anchors are added onto newly synthesized proteins in the ER. Thereby a putative transamidase removes a C-terminal peptide and attaches the truncated protein to the free amino group of the preformed GPI. The yeast mutant gpi8-1 is deficient in this addition of GPIs to proteins. GPI8 encodes for an essential 47 kDa type I membrane glycoprotein residing on the luminal side of the ER membrane. GPI8 shows significant homology to a novel family of vacuolar plant endopeptidases one of which is supposed to catalyse a transamidation step in the maturation of concanavalin A and acts as a transamidase in vitro. Humans have a gene which is highly homologous to GPI8 and can functionally replace it.
| Status: Published | Type: Journal Article | PubMed ID: 8978684 |
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| Topics | Genes linked to topics |
|---|---|
| GPI8 | |
| Cellular Location | |
| Cross-species Expression | |
| DNA/RNA Sequence Features | |
| Function/Process | |
| Mutants/Phenotypes | |
| Non-Fungal Related Genes/Proteins | |
| Primary Literature | |
| Protein Sequence Features | |
| Strains/Constructs | |




