Carroll SY~Drubin DG, 2009

Pubmed ID 19853568
Title A yeast killer toxin screen provides insights into a/b toxin entry, trafficking, and killing mechanisms.
Authors Susheela Y Carroll, Peter C Stirling, Helen E M Stimpson, Esther Giesselmann, Manfred J Schmitt, David G Drubin
Abstract Like Ricin, Shiga, and Cholera toxins, yeast K28 is an A/B toxin that depends on endocytosis and retrograde trafficking for toxicity. Knowledge of the specific proteins, lipids, and mechanisms required for trafficking and killing by these toxins remains incomplete. Since K28 is a model for clinically relevant toxins, we screened over 5000 yeast mutants, identifying 365 that affect K28 sensitivity. Hypersensitive mutants revealed cytoprotective pathways, including stress-activated signaling and protein degradation. Resistant mutants clustered to endocytic, lipid organization, and cell wall biogenesis pathways. Furthermore, GPI anchors and transcriptional regulation are important for K28-cell binding. Strikingly, the AP2 complex, which in metazoans links endocytic cargo to the clathrin coat, but had no assigned function in yeast, was critical for K28 toxicity. Yeast AP2 localizes to endocytic sites and has a cargo-specific function in K28 uptake. This comprehensive genetic analysis identified conserved processes important for A/B toxin trafficking and killing.
Citation Dev Cell 2009; 17:552-60
Data abstract Deletion collection was tested for sensitivity/resistance to viral K28 toxin.


Download the list of datasets
Paper Phenotype Condition Medium Collection Tested mutants Data Details
Carroll SY~Drubin DG, 2009 growth (area of killing zone) secreted K28 toxin MBA hap alpha ~4,806 Discrete

Curation history

Tested strains

June 4, 2020 To request.
June 19, 2020 Request sent.
July 3, 2020 Not available.


June 4, 2020 Clarification needed.
June 19, 2020 Request sent.
July 3, 2020 Ready to load.
July 3, 2020 Not available.
July 24, 2020 Loaded.