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PIG‐S and PIG‐T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8
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Many eukaryotic cell surface proteins are anchored to the plasma membrane via glycosylphosphatidylinositol (GPI). The GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with a substrate protein. It was known that the GPI transamidase is a complex containing GAA1 and GPI8. Here, we report two new components of this enzyme: PIG-S and PIG-T. To determine roles for PIG-S and PIG-T, we disrupted these genes in mouse F9 cells by homologous recombination. PIG-S and PIG-T knockout cells were defective in transfer of GPI to proteins, particularly in formation of the carbonyl intermediates. We also demonstrate that PIG-S and PIG-T form a protein complex with GAA1 and GPI8, and that PIG-T maintains the complex by stabilizing the expression of GAA1 and GPI8. Saccharomyces cerevisiae Gpi16p (YHR188C) and Gpi17p (YDR434W) are orthologues of PIG-T and PIG-S, respectively.
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“The five subunits of S. cerevisiae GPI-T are Gpi8 (which contains the catalytic active site), Gpi16, Gaa1, Gpi17, and Gab1 (88,92,93).”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [93]
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Metadata
- Authors
- Ohishi, K., Inoue, N., & Kinoshita, T.
- Affiliations
- Research Institute for Microbial Diseases, The University of Osaka (JP)
- Corresponding author
- Kinoshita, Taroh
- Venue
- The EMBO Journal
- Published
- 2001-08-01
- Volume
- 20
- Issue
- 15
- Pages
- 4088-4098
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC149153
- OpenAlex
- W2023359733
- Cited by
- 177
- References
- 42
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 11 · 2023: 5 · 2022: 8 · 2021: 15 · 2020: 15 · 2019: 7 · 2018: 6 · 2017: 11 · 2016: 2 · 2015: 8 · 2014: 9 · 2013: 10 · 2012: 5
- FWCI
- 2.83
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- glycosylphosphatidylinositol anchor, carbonyl intermediates, protein complexes, protein stability, cell surface proteins
- MeSH terms
- Acyltransferases, Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Cell Line, Cricetinae, Humans, Membrane Glycoproteins, Molecular Sequence Data, Saccharomyces cerevisiae, Cell Adhesion Molecules, CHO Cells, Glycosylphosphatidylinositols, DNA, Complementary, Aminoacyltransferases, Saccharomyces cerevisiae Proteins, Mice
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