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Article

Gpi17p does not stably interact with other subunits of glycosylphosphatidylinositol transamidase in Saccharomyces cerevisiae.

Biochimica et biophysica acta - 15 Jun 2005

Zhu Yonghua, Fraering Patrick, Vionnet Christine, Conzelmann Andreas

Abstract excerpt

Homologues of Gpi8p, Gaa1p, Gpi16p, Gpi17p, and Cdc91p are essential components of the GPI transamidase complex that adds glycosylphosphatidylinositols (GPIs 1) to newly synthesized proteins in the ER. In mammalian cells, these five subunits remain stably associated with each other in detergent. In yeast, we find no stable stoichiometric association of Gpi17p with the Gpi8p-Gpi16p-Gaa1p core in detergent...

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Identifiers

PMID: 15939668
DOI: 10.1016/j.bbalip.2005.05.001

Genes

GPI

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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