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Screening for protein targets for ubiquitination upon pathogen infection


In eukaryotes, the tagging of proteins with ubiquitin typically leads to their subsequent recognition and degradation by the 26S proteasome. The proteolysis of some proteins is triggered by distinct environmental and developmental cues to control the abundance of crucial cellular regulators. Protein ubiquitination can also be involved in protein activation, protein trafficking, DNA repair and regulation of transcription and translation via mono-ubiquitination and non-canonical ubiquitination.

In plants, genetic analysis has identified many ubiquitin/26S (Ub/26S) related genes that regulate various developmental pathways. Recent evidence indicates that protein ubiquitination plays a crucial role in plant disease resistance. However, only a few proteins targeted for ubiquitination upon specific stimuli and developmental processes were identified. No proteins, targeted for ubiquitination upon pathogen infection, were identified in plants. These proteins are potential repressors of defence responses that are removed by ubiquitin-mediated proteolysis, or proteins that need to be activated by mono-ubiquitination.

Therefore, developing novel systems for isolating and identifying plant ubiquitinated proteins is essential for furthering our understanding of the biological significance of the Ub/26S system in plant disease resistance and development.

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Norwich Research Park, Colney
United Kingdom