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Article

Two endoplasmic reticulum (ER) membrane proteins that facilitate ER-to-Golgi transport of glycosylphosphatidylinositol-anchored proteins.

Molecular biology of the cell - 1 Apr 1999

Barz W P, Walter P

Abstract excerpt

Many eukaryotic cell surface proteins are anchored in the lipid bilayer through glycosylphosphatidylinositol (GPI). GPI anchors are covalently attached in the endoplasmic reticulum (ER). The modified proteins are then transported through the secretory pathway to the cell surface. We have identified two genes in Saccharomyces cerevisiae, LAG1 and a novel gene termed DGT1 (for "delayed GPI-anchored protein...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 10198056
DOI: 10.1091/mbc.10.4.1043
PMCID: PMC25232

Genes

GPI

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Two endoplasmic reticulum (ER) membrane proteins that facilitate ER-to-Golgi transport of glycosylphosphatidylinositol-anchored proteins.PMID 10198056Read ↗

Yeast Gaa1p is required for attachment of a completed GPI anchor onto proteins.Semantic proximity Read ↗

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AtPGAP1 functions as a GPI inositol-deacylase required for efficient transport of GPI-anchored proteins.Semantic proximity Read ↗

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PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins.Semantic proximity Read ↗

A defect in GPI synthesis as a suggested mechanism for the role of ARV1 in intellectual disability and seizures.Semantic proximity Read ↗

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Quality Control of GPI-Anchored ProteinsSemantic proximity Read ↗

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Cdc1p is a Golgi-localized glycosylphosphatidylinositol-anchored protein remodelase.Semantic proximity Read ↗

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