Ubiquitin and proteasome pathways

The paper presents cryo-EM structures of the 26S proteasome in four conformational states to elucidate how ATP hydrolysis drives substrate translocation and deubiquitination.

The paper identifies HtsRC as a substrate of the CRL3Kelch ubiquitin ligase complex, showing its role in ring canal expansion through proteasomal degradation.

The paper uses mathematical modeling to show that Cand1 exchange activity creates a trade-off between ligase activity and receptor exchange, optimizing substrate degradation and enabling flexible CRL repertoire adjustment.

The paper shows that an 'invisible' conformation of ubiquitin enhances its phosphorylation by PINK1 through a dynamic equilibrium involving the Ser65 loop.

The paper shows that SUMO and ubiquitin-proteasome systems regulate meiotic prophase events in mouse by controlling protein turnover through RNF212 and HEI10.