期刊
VIRULENCE
卷 5, 期 2, 页码 365-370出版社
LANDES BIOSCIENCE
DOI: 10.4161/viru.27373
关键词
Candida glabrata; endoplasmic reticulum stress; unfolded protein response; regulated Ire1-dependent decay; Ire1; Hac1; calcineurin; Slt2; antifungal resistance; virulence
资金
- Japanese Ministry of Education, Culture, Sports, Science and Technology [24791027, 21390305]
- Grants-in-Aid for Scientific Research [21390305, 24791027] Funding Source: KAKEN
The maintenance of endoplasmic reticulum (ER) homeostasis is critical for numerous aspects of cell physiology. Eukaryotic cells respond to the accumulation of misfolded proteins in the ER (ER stress) by activating the unfolded protein response (UPR), an intracellular signaling pathway that adjusts the folding capacity of the ER. Recent studies of several pathogenic fungi have revealed that the UPR is important for antifungal resistance and virulence; therefore, the pathway has attracted much attention as a potential therapeutic target. While the UPR is highly conserved among eukaryotes, our group recently discovered that the pathogenic yeast Candida glabrata lacks the typical fungal UPR, but possesses alternative mechanisms to cope with ER stress. This review summarizes how C. glabrata responds to ER stress and discusses the impacts of ER quality control systems on antifungal resistance and virulence.
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