Evidence map›Paper›PMID 11598210›Full record

ArticleMolecular biology of the cell2001

The GPI transamidase complex of Saccharomyces cerevisiae contains Gaa1p, Gpi8p, and Gpi16p.

P Fraering, I Imhof, U Meyer, J M Strub, A van Dorsselaer, C Vionnet, A Conzelmann

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 113 citations in OpenAlex.

  1. Molecular Insights into Fungal Glycosylphosphatidylinositol Transamidase Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

P FraeringInstitute of Biochemistry, University of Fribourg, Chemin du Musée 5, CH-1700 Fribourg, Switzerland.
I Imhof
U Meyer
J M Strub
A van Dorsselaer
C Vionnet
A Conzelmann
University of Fribourg · CHLaboratoire de Spectrométrie Ionique et Moléculaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AminoacyltransferasesHexosyltransferasesAcyltransferasesAmino Acid SequenceCell Adhesion MoleculesEndoplasmic ReticulumLipidsMacromolecular SubstancesMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsMolecular Sequence DataProtein PrecursorsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsAcyltransferasesAminoacyltransferasesCell Adhesion MoleculesCOOH-terminal signal transamidasedolichyl-diphosphooligosaccharide - protein glycotransferaseGAA1 protein, S cerevisiaeGpi16 protein, S cerevisiaeGPI8 protein, S cerevisiaeHexosyltransferasesLipidsMacromolecular SubstancesMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsProtein PrecursorsSaccharomyces cerevisiae ProteinsSEC61 protein, S cerevisiaeSEC Translocation ChannelsTransferases

Identifiers

PMID11598210
PMCPMC60174
OpenAlexW2146697765

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.