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Purpose of Review <p>The 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.</p> Recent Findings <p>Core 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.</p> Summary <p>Understanding 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.</p>

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Unfolded Protein Response: a Key Coordinator of Endoplasmic Reticulum Stress and Pathogenicity in Human Fungal Pathogens

  • 期刊论文

  • 发表日期：

    2025年11月1日

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  • Catia Mota,
  • Eun Jung Thak,
  • Seon Woo Song,
  • Hyun Ah Kang

摘要

Purpose of Review

The 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 Findings

Core 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.

Summary

Understanding 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.