The Endoplasmic Reticulum Stress in Yeast and Fungal Cells

Dear Colleagues,

The endoplasmic reticulum (ER) is a membrane-surrounded cellular compartment in which secretory proteins are folded and modified before being transported to the cell surface. In addition, many lipidic molecules are biosynthesized on the ER membrane. The dysfunction or functional shortage of the ER, namely, ER stress, is accompanied by ER accumulation of unfolded proteins, which triggers a cytoprotective response called the unfolded protein response (UPR), commonly observed in eukaryotic cells. Although key players in the intracellular signaling pathway of the UPR, such as Ire1 and Hac1, have been identified through frontier studies using the yeast Saccharomyces cerevisiae as a model organism in the 1990s, intriguing new insights concerning the regulation of these UPR mediator are ongoingly reported. Another recent topic is the diversity of UPR signaling in yeast and fungal species, which means, for instance, that these UPR mediators do not exhibit the same function in different species. The relationship between virulence and UPR in pathogenic yeasts or fungi is also an important topic, as protein secretion is upregulated upon infection, leading to the induction of UPR. The ER is enforced and enlarged by the UPR. Therefore, it may also be possible to increase the industrial productivity of secretory proteins and/or lipidic molecules from yeasts and/or fungi through the artificial upregulation of the UPR.

This Special Issue focuses on current topics related to ER stress and UPR in yeasts and fungi from a wide range of viewpoints, including basic molecular biology, clinical science, and applicative technology. By gathering up-to-date insights from various research fields, I believe that we can illustrate the novel aspects of this intriguing theme.

Dr. Yukio Kimata
Guest Editor

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• unfolded protein response
• yeast
• fungi
• endoplasmic reticulum
• protein production