title: ER stress response mechanisms in the pathogenic yeast Candida glabrata and their roles in virulence.
abstract: 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.
authors: Department of Molecular Microbiology and Immunology; Nagasaki University School of Medicine; Nagasaki, Japan; Department of Respiratory Medicine; Sasebo City General Hospital; Nagasaki, Japan.
authors: Taiga
authors: T
authors: Miyazaki
authors: Department of Molecular Microbiology and Immunology; Nagasaki University School of Medicine; Nagasaki, Japan.
authors: Shigeru
authors: S
authors: Kohno
mesh_terms: D000935:Antifungal Agents / Q000378:metabolism; D041221:Candida glabrata / Q000187:drug effects / Q000472:pathogenicity* / Q000502:physiology*; D004721:Endoplasmic Reticulum / Q000502:physiology*; D013312:Stress, Physiological; D056811:Unfolded Protein Response; D014774:Virulence
chemical_list: D000935:Antifungal Agents
keywords: Candida glabrata; Hac1; Ire1; Slt2; antifungal resistance; calcineurin; endoplasmic reticulum stress; regulated Ire1-dependent decay; unfolded protein response; virulence