Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins.

doi:10.1091/mbc.11.5.1523

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

Back to search

Article

Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins.

Molecular biology of the cell - 1 May 2000

Ohishi K, Inoue N, Maeda Y, Takeda J, Riezman H, Kinoshita T

Abstract excerpt

Many eukaryotic cell surface proteins are anchored to the membrane via glycosylphosphatidylinositol (GPI). The GPI is attached to proteins that have a GPI attachment signal peptide at the carboxyl terminus. The GPI attachment signal peptide is replaced by a preassembled GPI in the endoplasmic reticulum by a transamidation reaction through the formation of a carbonyl intermediate. GPI transamidase is a key enzyme...

Topics

Acyltransferases
Amino Acid Sequence
Aminoacyltransferases
Animals
Cell Adhesion Molecules
Cells, Cultured
Conserved Sequence
Glycosylphosphatidylinositols
Humans
Membrane Glycoproteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mice

Molecular Sequence Data

Mutation

Protein Precursors

Protein Sorting Signals

Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 10793132
DOI: 10.1091/mbc.11.5.1523
PMCID: PMC14864

Genes

GPI
GPAA1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins.PMID 10793132Read ↗

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

A conserved proline in the last transmembrane segment of Gaa1 is required for glycosylphosphatidylinositol (GPI) recognition by GPI transamidase.Semantic proximity Read ↗

Functional Analysis of the GPI Transamidase Complex by Screening for Amino Acid Mutations in Each Subunit.Semantic proximity Read ↗

Human PIG-U and Yeast Cdc91p Are the Fifth Subunit of GPI Transamidase That Attaches GPI-Anchors to ProteinsSemantic proximity Read ↗

Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins.Semantic proximity Read ↗

The Schizosaccharomyces pombe GPI8 gene complements a Saccharomyces cerevisiae GPI8 anchoring mutant.Semantic proximity Read ↗

Mutations in GPAA1, Encoding a GPI Transamidase Complex Protein, Cause Developmental Delay, Epilepsy, Cerebellar Atrophy, and Osteopenia.Semantic proximity Read ↗

Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain.Semantic proximity Read ↗

Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge.Semantic proximity Read ↗

GPI Transamidase and GPI anchored proteins: Oncogenes and biomarkers for cancerSemantic proximity Read ↗

Subunits of the GPI transamidase complex localize to the endoplasmic reticulum and nuclear envelope in Drosophila.Semantic proximity Read ↗

Molecular insights into biogenesis of glycosylphosphatidylinositol anchor proteinsSemantic proximity Read ↗

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