Evidence map›Paper›PMID 40557545›Full record

ArticleJournal of cell science2025

Killer toxin K28 resistance in yeast relies on COG complex-mediated trafficking of the defence factor Ktd1.

Kamilla M E Laidlaw, Hatwan H Nadir, Amy Milburn, Martha S C Xelhuantzi, Justas Stanislovas, Alastair P Droop, Sandy MacDonald, Ilya Andreev, Andrew Leech, Daniel Ungar and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cell science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. A Comprehensive Structural and Functional Analysis ofbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
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

12 authors.

Kamilla M E LaidlawYork Biomedical Research Institute and Department of Biology, University of York, York YO10 5DD, UK.
Hatwan H NadirYork Biomedical Research Institute and Department of Biology, University of York, York YO10 5DD, UK.
Amy MilburnYork Biomedical Research Institute and Department of Biology, University of York, York YO10 5DD, UK.
Martha S C XelhuantziYork Biomedical Research Institute and Department of Biology, University of York, York YO10 5DD, UK.
Justas StanislovasYork Biomedical Research Institute and Department of Biology, University of York, York YO10 5DD, UK.
Alastair P DroopBioscience Technology Facility, Department of Biology, University of York, York YO10 5DD, UK.
Sandy MacDonaldBioscience Technology Facility, Department of Biology, University of York, York YO10 5DD, UK.
Ilya AndreevCentre for Genomics & Data Science Research, National Human Genome Research Institute, NIH, Bethesda, MD 20892, USA.
Andrew LeechBioscience Technology Facility, Department of Biology, University of York, York YO10 5DD, UK.
Daniel UngarYork Biomedical Research Institute and Department of Biology, University of York, York YO10 5DD, UK.
Meru J SadhuCentre for Genomics & Data Science Research, National Human Genome Research Institute, NIH, Bethesda, MD 20892, USA.
Chris MacDonaldYork Biomedical Research Institute and Department of Biology, University of York, York YO10 5DD, UK.ORCID 0000-0002-7450-600X

Funding

NIH HHSRoyal Society 204636/Z/16/ZUniversity of YorkWellcome TrustWellcome Trust 204636/Z/16/Z
6 · The paper itself

Abstract

AB toxins are a diverse family of protein toxins that enter host cells via endocytosis and induce cell death. In yeast, the AB toxin K28 is internalised to endosomes of susceptible yeast, before following the retrograde trafficking pathway and ultimately triggering cell cycle arrest. The endolysosomal defence factor Ktd1 protects against K28, but its regulation remains unclear. We show all lobe B subunits of the conserved oligomeric Golgi (COG) tethering complex are required for K28 resistance. Our experiments suggest the hypersensitivity of cog mutants is primarily explained by defects in Ktd1 trafficking. Ktd1 mis-localisation in cog mutants is reminiscent of disruptions in Snc1, a surface cargo that recycles multiple times via the Golgi. This work suggests not only that the COG complex is responsible for the precise trafficking of Ktd1 required to mediate toxin defence, but that Ktd1 might survey endolysosomal compartments for toxin. This work underpins the importance of Ktd1 in defence against the AB toxin K28, and implies how various membrane trafficking regulators could influence toxin effects in other eukaryotic systems.

Indexed as

Adaptor Proteins, Vesicular TransportKiller Factors, YeastSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEndocytosisEndosomesGolgi ApparatusMutationProtein TransportAdaptor Proteins, Vesicular TransportKiller Factors, YeastSaccharomyces cerevisiae ProteinsAB toxinsCOG complexEndolysosomesK28Killer toxinsMembrane trafficking

Identifiers

PMID40557545
PMCPMC12301656

What OpenQuestion holds

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Registered trials

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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.