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    EMBO J. 1996 Dec 2;15(23):6575-83.

    Yeast Gpi8p is essential for GPI anchor attachment onto proteins.

    Benghezal M, Benachour A, Rusconi S, Aebi M, Conzelmann A.

    Source

    Institute of Biochemistry, University of Fribourg, Perolles, Switzerland.

    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.

    PMID:
    8978684
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC452482
    Free PMC Article

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