Ubiquitin and proteasome pathways

The paper determines the crystal structure of the KLHL20-DAPK1 complex, revealing the molecular basis of DAPK1 recruitment to the KLHL20 E3 ligase and suggesting a novel target for PROTAC-based drug design.

This study identifies Gcn5 and Ubp8-dependent ubiquitylation of glycolytic enzymes in yeast, linking epigenetic regulation to metabolic function.

The paper shows that NEDP1 regulates the NEDD8 cycle upon DNA damage, modulating HSP70 ATPase activity to promote apoptosis and identifies this as relevant in hepatocellular carcinoma.

This study identifies a family of FYVE-type-RING finger proteins as E3 ligases that cooperate with Ubc13-Mms2 in K63-polyubiquitylation at internal membranes across species.

The paper identifies degrons and E3 ligase alterations across cancer types, finding that at least 1 in 7 driver mutations affect these components.

The paper identifies RUVBL1 and TIP60 as essential regulators of Nrf1-mediated transcription of proteasome genes, showing their role in cellular response to proteotoxic stress.

The paper shows that Cdt2 binds PCNA via a PIP box, enhancing CRL4Cdt2 activity and Cdt1 ubiquitination, suggesting a new mechanism for substrate targeting.

The paper identifies K63 ubiquitination sites on ribosomes in yeast under oxidative stress using mass spectrometry, revealing their role in post-initiation translation control.

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 shows that mitotic replisome disassembly in vertebrates depends on TRAIP-mediated ubiquitylation of Mcm7 and p97/VCP activity, and is conserved across higher eukaryotes.

The paper identifies USP21 and OTUD3 as deubiquitylating enzymes that counteract ZNF598-mediated ribosomal ubiquitylation, facilitating ribosome-associated quality control.

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 identifies PSMA3 as a receptor for 20S proteasome-mediated degradation of intrinsically disordered proteins (IDPs) and shows its C-terminal fragment inhibits IDP degradation.

iSUMO integrates sequence and protein features to predict functional SUMOylation events, identifying more targets in human and yeast than existing tools at the same false positive rate.

The paper re-analyzes protein half-life data in yeast to provide consistent estimates, finding that protein stability correlates with abundance and function.

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