ArticleEukaryotic cell2005
Gpi19, the Saccharomyces cerevisiae homologue of mammalian PIG-P, is a subunit of the initial enzyme for glycosylphosphatidylinositol anchor biosynthesis.
Article in Eukaryotic cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 32 citations in OpenAlex.
- An Investigation of TDA1 Deficiency in Saccharomyces cerevisiae During Diauxic Growth.Yeast (Chichester, England) · 2025Article
- Immune Reactivity to Raw and Processed Foods and Their Possible Contributions to Autoimmunity.Foods (Basel, Switzerland) · 2025Review
- Glycosylphosphatidylinositol Anchor Biosynthesis Pathway-Related Protein GPI7 Is Required for the Vegetative Growth and Pathogenicity ofInternational journal of molecular sciences · 2022Article
- Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host.Journal of fungi (Basel, Switzerland) · 2021Review
- Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast.International journal of molecular sciences · 2021Review
- Ras signaling activates glycosylphosphatidylinositol (GPI) anchor biosynthesis via the GPI-The Journal of biological chemistry · 2018Article
- A Lipid Transfer Protein Signaling Axis Exerts Dual Control of Cell-Cycle and Membrane Trafficking Systems.Developmental cell · 2018Article
- Saccharomyces cerevisiae Gpi2, an accessory subunit of the enzyme catalyzing the first step of glycosylphosphatidylinositol (GPI) anchor biosynthesis, selectively complements some of the functions of its homolog in Candida albicans.Glycoconjugate journal · 2014Article
- Comparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans.International journal of microbiology · 2014Review
- Review
- Protein Glycosylation in Aspergillus fumigatus Is Essential for Cell Wall Synthesis and Serves as a Promising Model of Multicellular Eukaryotic Development.International journal of microbiology · 2012Article
- Identification of positive regulators of the yeast fps1 glycerol channel.PLoS genetics · 2009Article
- The Aspergillus nidulans pigP gene encodes a subunit of GPI-N-acetylglucosaminyltransferase which influences filamentation and protein secretion.Current genetics · 2009Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Glycosylphosphatidylinositols (GPIs) are attached to the C termini of some glycosylated secretory proteins, serving as membrane anchors for many of those on the cell surface. Biosynthesis of GPIs is initiated by the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to phosphatidylinositol. This reaction is carried out at the endoplasmic reticulum (ER) by an enzyme complex called GPI-N-acetylglucosaminyltransferase (GPI-GlcNAc transferase). The human enzyme has six known subunits, at least four of which, GPI1, PIG-A, PIG-C, and PIG-H, have functional homologs in the budding yeast Saccharomyces cerevisiae. The uncharacterized yeast gene YDR437w encodes a protein with some sequence similarity to human PIG-P, a fifth subunit of the GPI-GlcNAc transferase. Here we show that Ydr437w is a small but essential subunit of the yeast GPI-GlcNAc transferase, and we designate its gene GPI19. Similar to other mutants in the yeast enzyme, temperature-sensitive gpi19 mutants display cell wall defects and hyperactive Ras phenotypes. The Gpi19 protein associates with the yeast GPI-GlcNAc transferase in vivo, as judged by coimmuneprecipitation with the Gpi2 subunit. Moreover, conditional gpi19 mutants are defective for GPI-GlcNAc transferase activity in vitro. Finally, we present evidence for the topology of Gpi19 within the ER membrane.
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