Evidence map›Paper›PMID 15470244›Full record

ArticleEukaryotic cell2004

Pmt-mediated O mannosylation stabilizes an essential component of the secretory apparatus, Sec20p, in Candida albicans.

Yvonne Weber, Stephan K-H Prill, Joachim F Ernst

Abstract read
In one paragraph

Article in Eukaryotic cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Extension ofmBio · 2022
    Article
  2. Monitoring Protein Dynamics in ProteinMolecules (Basel, Switzerland) · 2018
    Article
  3. Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae.Molecular & cellular proteomics : MCP · 2016
    Article
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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

3 authors.

Yvonne WeberInstitut für Mikrobiologie Heinrich-Heine-Universität Düsseldorf, Universitätsstr. 1/Geb. 26.12, D-40225 Düsseldorf, Germany.
Stephan K-H Prill
Joachim F Ernst

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sec20p is an essential endoplasmic reticulum (ER) membrane protein in yeasts, functioning as a tSNARE component in retrograde vesicle traffic. We show that Sec20p in the human fungal pathogen Candida albicans is extensively O mannosylated by protein mannosyltransferases (Pmt proteins). Surprisingly, Sec20p occurs at wild-type levels in a pmt6 mutant but at very low levels in pmt1 and pmt4 mutants and also after replacement of specific Ser/Thr residues in the lumenal domain of Sec20p. Pulse-chase experiments revealed rapid degradation of unmodified Sec20p (38.6 kDa) following its biosynthesis, while the stable O-glycosylated form (50 kDa) was not formed in a pmt1 mutant. These results suggest a novel function of O mannosylation in eukaryotes, in that modification by specific Pmt proteins will prevent degradation of ER-resident membrane proteins via ER-associated degradation or a proteasome-independent pathway.

Indexed as

Amino Acid SequenceBinding SitesCandida albicansFungal ProteinsGenes, FungalGlycosylationHumansMannoseMannosyltransferasesMembrane GlycoproteinsMolecular Sequence DataMutationUbiquitinVesicular Transport ProteinsFungal ProteinsMannoseMannosyltransferasesMembrane Glycoproteinsprotein O-mannosyltransferaseUbiquitinVesicular Transport Proteins

Identifiers

PMID15470244
PMCPMC522601

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.