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The Universal Stress Protein SlUSP1 modulates Botrytis cinerea resistance via ATP-dependent chitinase activation in tomato
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DOI：10.1016/j.plantsci.2026.113292.png)
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Abstract
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• SlUSP1, a cytoplasmic-localized universal stress protein, functions as a positive regulator of Botrytis cinerea resistance in tomato. • SlUSP1 forms homodimers and interacts with the CRL4 complex adaptors SlWDR23 and SlWDR110, which mediate its degradation via the 26S proteasome pathway. • Botrytis cinerea infection suppresses SlWDR23 and SlWDR110, thereby stabilizing SlUSP1 as part of the host defense response. • SlUSP1 enhances chitinase activity in an ATP-dependent manner, thereby conferring resistance to Botrytis cinerea. • Establishes the CRL4SlWDR23/SlWDR110-SlUSP1-chitinase regulatory mechanism in tomato antifungal defense.
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