Journal
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY
Volume 308, Issue 3, Pages 378-386Publisher
ELSEVIER GMBH
DOI: 10.1016/j.ijmm.2018.03.004
Keywords
Stress-associated endoplasmic reticulum protein 1 (SERP1); Atg8; Unfolded protein response (UPR); ER stress; Virulence
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Funding
- National Natural Science Foundation of China [31670146, 81471923, 31400132]
- Natural Science Foundation of Tianjin [17JCZDJC33300, 15JCQNJC09300]
- Open Fund of Ministry of Education Key Laboratory of Moleular Microbiology and Technology, Nankai University
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Cellular stresses could activate several response processes, such as the unfolded protein response (UPR), autophagy and oxidative stress response to restore cellular homeostasis or render cell death. Herein, we identified the Candida albicans stress-associated endoplasmic reticulum protein 1 (SERP1), also known as Ysy6, which was involved in endoplasmic reticulum (ER) stress response. We found that deletion of both SERP1/YSY6 and ATG8 led to hypersensitivity to tunicamycin (TN), and resulted in severe mitochondrial dysfunction under this stress. UPR reporting systems illustrated that the double mutation attenuated splicing of HAC1 mRNA, followed by decreased level of UPR activation. In addition, the atg8 Delta/Delta ysy6 Delta/Delta double mutant had normal autophagic degradation of the ER component Sec63 under ER stress, suggesting that SERP1/Ysy6 and Atg8 synergistically regulated UPR that is independent on autophagy. We also found that deletion of both SERP1/YSY6 and ATG8 caused the loss of virulence. This study reveals the important role of SERP1/Ysy6 and Atg8 in ER stress response and virulence in C. albicans.
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