ArticleCommunications biology2025
GSK3 phosphorylates and activates trehalose-6-phosphate synthase to improve trehalose production and thermotolerance in Ganoderma lucidum.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Glutathione peroxidase gene regulates heat stress response via trehalose synthesis in Pleurotus ostreatus.Applied microbiology and biotechnology · 2026Article
- Unraveling the Signaling Networks: How Exogenous Substances Mitigate Heat Stress in Edible Fungi.Journal of fungi (Basel, Switzerland) · 2026Review
- Multi-omics analysis of polysaccharide accumulation and associated metabolic reprogramming across developmental stages ofFrontiers in microbiology · 2026Article
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Authors and funding
10 authors.
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Abstract
Glycogen synthase kinase 3 (GSK3) plays crucial roles in diverse organisms, yet its physiological functions in filamentous fungi remain poorly characterized. Here, we show that knockdown of GlGSK3 in Ganoderma lucidum leads to increased glycogen accumulation, reduced pyruvate and ATP production, and impaired hyphal growth and thermotolerance. GlGSK3 interacts with and phosphorylates trehalose-6-phosphate synthase (TPS) at Serine 529, enhancing its enzymatic activity. Consistent with the central role of TPS in trehalose biosynthesis, trehalose levels were significantly lower in gltps-kd and glgsk3-kd strains compared to the wild type. Similarly, gltps-kd strains also exhibited diminished hyphal growth and thermotolerance. Under heat stress, both GlGSK3 and GlTPS protein levels were upregulated, leading to increased GlTPS phosphorylation, enhanced enzymatic activity, and elevated trehalose accumulation. Together, these results uncover a key role for GlGSK3 and the GSK3-TPS module in G. lucidum in regulating growth and adaptation to environmental stress.
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