A NACHT domain-containing protein Ncp is required for appendage-associated unconventional protein secretion in the fungus Penicillium herquei
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Updated: Jul 1, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
Luwen Yan1, Wei Deng1, Penglei Qiu1
1State Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Molecular Microbiology and Technology of the Ministry of Education, Department of Microbiology, Frontiers Science Center for Cell Responses, College of Life Science, Nankai University, Tianjin 300071, China.
Abstract:
Unconventional protein secretion (UcPS) enables leaderless proteins to bypass the ER-Golgi pathway, yet its regulation in fungi is not fully characterized. Here, we identify an appendage-associated secretion route in the symbiotic fungus Penicillium herquei Ph506 that mediates the extracellular accumulation of leaderless proteins. Functional analyses reveal that Ncp, a highly upregulated NACHT domain-containing protein, is dispensable for appendage formation but required for the efficient secretion of leaderless proteins into these specialized structures under tested conditions. Notably, Ncp depletion suppresses programmed cell death (PCD) features and reduces ionic stress tolerance, suggesting a potential link between NACHT-mediated processes and stress-associated cellular states. Together, this work provides evidence of a specific regulatory mechanism for protein secretion in symbiotic fungi, offering insights into how PCD-related pathways and UcPS may be co-regulated to maintain cellular homeostasis.
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