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Cited by 111Glycosylation and Glycoproteins ResearchFungal and yeast genetics researchCellular transport and secretion

The GPI Transamidase Complex of Saccharomyces cerevisiae Contains Gaa1p, Gpi8p, and Gpi16p

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Fraering, Patrick, Imhof, Isabella, Meyer, Urs, Strub, Jean-Marc, van Dorsselaer, Alain, Vionnet, Christine, Conzelmann, Andreas·2001·Molecular Biology of the Cell
DOI 10.1091/mbc.12.10.3295PMC PMC60174
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Abstract

Gpi8p and Gaa1p are essential components of the GPI transamidase that adds glycosylphosphatidylinositols (GPIs) to newly synthesized proteins. After solubilization in 1.5% digitonin and separation by blue native PAGE, Gpi8p is found in 430–650-kDa protein complexes. These complexes can be affinity purified and are shown to consist of Gaa1p, Gpi8p, and Gpi16p (YHR188c). Gpi16p is an essential N-glycosylated transmembrane glycoprotein. Its bulk resides on the lumenal side of the ER, and it has a single C-terminal transmembrane domain and a small C-terminal, cytosolic extension with an ER retrieval motif. Depletion of Gpi16p results in the accumulation of the complete GPI lipid CP2 and of unprocessed GPI precursor proteins. Gpi8p and Gpi16p are unstable if either of them is removed by depletion. Similarly, when Gpi8p is overexpressed, it largely remains outside the 430–650-kDa transamidase complex and is unstable. Overexpression of Gpi8p cannot compensate for the lack of Gpi16p. Homologues of Gpi16p are found in all eucaryotes. The transamidase complex is not associated with the Sec61p complex and oligosaccharyltransferase complex required for ER insertion and N-glycosylation of GPI proteins, respectively. When GPI precursor proteins or GPI lipids are depleted, the transamidase complex remains intact.

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  • S. cerevisiae GPI-T can be purified as a core heterotrimer containing only Gpi8, Gpi16, and Gaa1.

    “S. cerevisiae GPI-T can be purified as a core heterotrimer, containing only Gpi8, Gpi16, and Gaa1 (92)”

    From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [92]

  • The five subunits of S. cerevisiae GPI-T are Gpi8 (containing the catalytic active site), Gpi16, Gaa1, Gpi17, and Gab1.

    “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 [92]

  • In vivo, GPI-T is expected to be a dimer of pentamers, with dimerization occurring on one face of the caspase-like Gpi8 subunit.

    “In vivo, GPI-T is expected to be a dimer of pentamers, with dimerization occurring on one face of the caspase-like Gpi8 subunit (92,97,98).”

    From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [92]

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Authors
Fraering, P., Imhof, I., Meyer, U., Strub, J.-M., van Dorsselaer, A., Vionnet, C., & Conzelmann, A.
Affiliations
  • University of Fribourg (CH)
  • Centre National de la Recherche Scientifique (FR)
  • Laboratoire de Spectrométrie de Masse Bio-Organique, UMR CNRS 7509, 67008 Strasbourg Cedex, France
ORCID
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2001-10
Volume
12
Issue
10
Pages
3295-3306
ISSN
  • 1059-1524 (ISSN-L)
  • 1939-4586
DOI
10.1091/mbc.12.10.3295
PMC
PMC60174
OpenAlex
W2146697765
Cited by
111
References
39
Citations by year
2025: 1 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 7 · 2020: 6 · 2019: 1 · 2018: 2 · 2017: 4 · 2016: 2 · 2015: 3 · 2014: 4 · 2013: 6 · 2012: 4
FWCI
3.62
Type
journal article
Language
en
Open access
Locations
  • Molecular Biology of the Cell (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
  • Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
glycosylphosphatidylinositol, endoplasmic reticulum, transmembrane glycoprotein, protein complex stability, Saccharomyces cerevisiae, N-glycosylation, oligosaccharyltransferase
MeSH terms
SEC Translocation Channels, Acyltransferases, Amino Acid Sequence, Endoplasmic Reticulum, Hexosyltransferases, Lipids, Membrane Glycoproteins, Membrane Proteins, Molecular Sequence Data, Protein Precursors, Saccharomyces cerevisiae, Transferases, Cell Adhesion Molecules, Aminoacyltransferases, Membrane Transport Proteins, Saccharomyces cerevisiae Proteins, Macromolecular Substances

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