ScholarWorks@중앙대학교

초록

Purpose of ReviewThe unfolded protein response (UPR) is essential for maintaining endoplasmic reticulum (ER) homeostasis during stress. In fungal pathogens, UPR contributes not only to protein folding and degradation but also to stress resilience, immune evasion, and virulence. This review aimed to explore the functional significance of UPR and its coordination with ER-associated degradation (ERAD) and ER-protein quality control (ERQC) in clinically relevant fungal pathogens.Recent FindingsCore UPR regulators mediate fungal adaptation to host-imposed stress by modulating glycoprotein processing, secretion, and cell wall integrity. Targeting UPR, ERAD, or ERQC components enhances antifungal susceptibility and disrupts fungal pathogenesis. However, the precise molecular roles of evolutionarily conserved and diverged UPR components, the integration of UPR with other stress-response pathways, and the need for pathogen-specific exploration to understand unique adaptations and regulatory mechanisms remain to be elucidated.SummaryUnderstanding the UPR-ERAD-ERQC network reveals new therapeutic vulnerabilities of fungal pathogens. The pharmacological disruption of these pathways may bolster antifungal efficacy and help counter rising drug resistance.

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