Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Pga1 is an essential component of Glycosylphosphatidylinositol-mannosyltransferase II of Saccharomyces cerevisiae.

Molecular biology of the cell - 1 Sept 2007

Sato Keisuke, Noda Yoichi, Yoda Koji

Abstract excerpt

The Saccharomyces cerevisiae essential gene YNL158w/PGA1 encodes an endoplasmic reticulum (ER)-localized membrane protein. We constructed temperature-sensitive alleles of PGA1 by error-prone polymerase chain reaction mutagenesis to explore its biological role. Pulse-chase experiments revealed that the pga1(ts) mutants accumulated the ER-form precursor of Gas1 protein at the restrictive temperature. Transport of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Endoplasmic Reticulum
Share to Enzyme Stability
Share to Glycosylphosphatidylinositols

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

Share to Mannosyltransferases

Share to Microbial Viability

Share to Mutant Proteins

Share to Protein Precursors

Share to Protein Subunits

Source

Open in PubMed Open full text

Identifiers

PMID: 17615295
DOI: 10.1091/mbc.e07-03-0258
PMCID: PMC1951765

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Pga1 is an essential component of Glycosylphosphatidylinositol-mannosyltransferase II of Saccharomyces cerevisiae.PMID 17615295Read ↗

Gpi1, a Saccharomyces cerevisiae protein that participates in the first step in glycosylphosphatidylinositol anchor synthesis.Semantic proximity Read ↗

Characterization of GPI14/YJR013w mutation that induces the cell wall integrity signalling pathway and results in increased protein production in Saccharomyces cerevisiae.Semantic proximity Read ↗

GUP1 of Saccharomyces cerevisiae encodes an O-acyltransferase involved in remodeling of the GPI anchor.Semantic proximity Read ↗

Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are defective in the synthesis of N-acetylglucosaminyl phosphatidylinositol. Cloning of the GPI2 gene.Semantic proximity Read ↗

Glycosylphosphatidylinositol biosynthesis defects in Gpi11p- and Gpi13p-deficient yeast suggest a branched pathway and implicate gpi13p in phosphoethanolamine transfer to the third mannose.Semantic proximity Read ↗

Yeast ARV1 is required for efficient delivery of an early GPI intermediate to the first mannosyltransferase during GPI assembly and controls lipid flow from the endoplasmic reticulum.Semantic proximity Read ↗

Mutations that are synthetically lethal with a gas1Delta allele cause defects in the cell wall of Saccharomyces cerevisiae.Semantic proximity Read ↗

Gpi17p does not stably interact with other subunits of glycosylphosphatidylinositol transamidase in Saccharomyces cerevisiae.Semantic proximity Read ↗

Cdc1 removes the ethanolamine phosphate of the first mannose of GPI anchors and thereby facilitates the integration of GPI proteins into the yeast cell wall.Semantic proximity Read ↗

Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast.Semantic proximity Read ↗

Defects in protein glycosylation cause SHO1-dependent activation of a STE12 signaling pathway in yeast.Semantic proximity Read ↗

A conditionally lethal yeast mutant blocked at the first step in glycosyl phosphatidylinositol anchor synthesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.