Ubiquitin and proteasome pathways

This study shows UBQLN2 stabilizes substrates by recruiting E3 ligases, which promotes phase separation and protects against proteasomal degradation, and this mechanism is disrupted in ALS mutants.

The paper identifies Muskelin as a substrate adaptor for the Drosophila CTLH E3 ligase, showing how it regulates the degradation of RNA-binding proteins during the maternal-to-zygotic transition.

This study elucidates how BACH1 is regulated by SCFFBXO22 and SCFFBXL17 through structural changes in FBXO22 and modifications in BACH1's BTB domain, affecting its ubiquitylation and stability.

The paper identifies TRIM52 as a primate-specific DNA repair factor under tight proteolytic control by BIRC6, HUWE1, and UBR4/KCMF1.

This study quantifies site-specific ribosome ubiquitination under oxidative stress and identifies stress-specific ubiquitin modification patterns.

This paper identifies engineered ubiquitin variants that suppress Salmonella NEL SspH1 toxicity in yeast by modulating ubiquitination activity and cell cycle interference.

This study uses molecular dynamics simulations to investigate how the BRCA1/BARD1-UbcH5c complex ubiquitinates H2A, highlighting the role of H3 in orienting the E2-Ub complex.

This study identifies HOIP and linear ubiquitin chains as critical for TRIM21-mediated ADIN by recruiting VCP, enhancing virus neutralization.

The paper shows that loss of FBXO2 promotes hepatocellular carcinoma by stabilizing Hsp47 through SKP2-mediated proteasomal degradation.

The paper develops an Arg-mediated N-end rule assay system to show that deamidase expression levels regulate protein degradation via the N-end rule pathway.

The paper shows that the CTLH E3 ligase complex regulates substrate selectivity and autoregulation by exchanging its β-propeller subunits WDR26 and muskelin.

The paper develops subunit-specific proteasome substrates for Schistosoma species, showing improved performance and cross-species applicability.

The paper identifies the intrinsically disordered N-terminus of SUMO1 as an intramolecular inhibitor of SUMO-SIM interactions, revealing a mechanism of disorder-based autoinhibition.

This study compares the expression of three HECT E3 ligases in E. coli, finding that lower temperatures improve solubility and yield, while full-length proteins are less successfully expressed than isolated domains.

This study identifies UBE2D/eff as critical for maintaining proteostasis and a youthful proteome during aging by regulating protein degradation and preventing aggregate accumulation.

This study identifies age-related changes in ubiquitylation, acetylation, and phosphorylation sites in mouse brains and finds conserved effects in killifish, linking proteasome inhibition to aging ubiquitylome remodeling.

This study identifies a domain in RNF216 that regulates dendritic arborization and spine morphology through ubiquitin chain assembly, independent of its catalytic activity.

This paper identifies and characterizes selective Smurf1 inhibitors that block the trans-thiolation reaction, showing high selectivity over Smurf2.

The paper shows that ubiquitination of nascent proteins by LTN1 is reversed by deubiquitinases, allowing maturation of correctly folded proteins while misfolded ones are degraded.

The paper identifies a conserved N-terminal motif in CUL3 that mediates dimerization and activates CRL3KLHL22 E3 ligase function.

This study shows NatB-dependent acetylation protects procaspase-8 from degradation by UBR4, which is essential for full extrinsic apoptosis.

This study identifies USP48 as a nuclear deubiquitinase that regulates synapse remodeling by promoting spine pruning and reducing synaptic protein clustering.

This paper identifies VCF1 as a novel p97 cofactor that enhances p97-UFD1-NPL4 interactions with ubiquitylated substrates, promoting proteasomal degradation.

The paper identifies NFATC2IP as a mediator of SUMO-dependent genome integrity through CRISPR/Cas9 screens and functional validation.

This paper identifies HUWE1 as a ubiquitin ligase that enhances ubiquitin modifications on proteins and aggregates, promoting their degradation via proteasome and autophagy pathways.

The paper investigates how ZFAND5 activates the 26S proteasome by inducing conformational changes that enhance substrate degradation.

This study identifies a bi-functional N-terminal degradation control sequence in REV-ERBα that regulates its ubiquitination and degradation through interactions with E3 ligases.

This study shows that immunoproteasome deficiency accelerates brain aging and causes epilepsy in mice, with reduced immunoproteasome expression also observed in human epilepsy patients.

The paper identifies lysine deserts in UPS components across species and shows they can be regulated by non-lysine ubiquitination and ubiquitin-independent proteasomal degradation.

The paper identifies a small molecule DUB probe, IMP-2373, that quantitatively engages multiple DUBs in live cells and demonstrates its use in studying DUB activity changes during MYC deregulation.