Hwang G~Naganuma A, 2014

Pubmed ID 25074250
Title The protein transportation pathway from Golgi to vacuoles via endosomes plays a role in enhancement of methylmercury toxicity.
Authors Gi-Wook Hwang, Yasutaka Murai, Tsutomu Takahashi, Akira Naganuma
Abstract Methylmercury causes serious damage to the central nervous system, but the molecular mechanisms of methylmercury toxicity are only marginally understood. In this study, we used a gene-deletion mutant library of budding yeast to conduct genome-wide screening for gene knockouts affecting the sensitivity of methylmercury toxicity. We successfully identified 31 genes whose deletions confer resistance to methylmercury in yeast, and 18 genes whose deletions confer hypersensitivity to methylmercury. Yeast genes whose deletions conferred resistance to methylmercury included many gene encoding factors involved in protein transport to vacuoles. Detailed examination of the relationship between the factors involved in this transport system and methylmercury toxicity revealed that mutants with loss of the factors involved in the transportation pathway from the trans-Golgi network (TGN) to the endosome, protein uptake into the endosome, and endosome-vacuole fusion showed higher methylmercury resistance than did wild-type yeast. The results of our genetic engineering study suggest that this vesicle transport system (proteins moving from the TGN to vacuole via endosome) is responsible for enhancing methylmercury toxicity due to the interrelationship between the pathways. There is a possibility that there may be proteins in the cell that enhance methylmercury toxicity through the protein transport system.
Citation Sci Rep 2014; 4:5888


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Paper Phenotype Condition Medium Collection Tested mutants Data Details
Hwang G~Naganuma A, 2014 growth (culture turbidity) methylmercury chloride [60 nM] SD hap alpha ~4,850 Quantitative only for hits

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June 23, 2020 To request.
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June 23, 2020 To request.
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