Ubiquitin and proteasome pathways

This paper shows that the ASB9-CRL ubiquitin ligase polyubiquitylates histones H3 and H4, but not H2A and H2B, and that this process requires ARIH2 and occurs only on free histones.

The paper solves high-resolution structures of TXNL1 bound to the human 26S proteasome, revealing conformation-specific binding and new insights into ATP hydrolysis and substrate translocation mechanisms.

This study characterizes a ubiquitin E3 RING ligase from Simkania negevensis, showing it generates K63- and K11-linked ubiquitin chains and interacts with specific E2 ligases.

This study characterizes the Bub bacterial ubiquitination-like pathway, revealing its unique biochemical mechanisms and structural similarities to eukaryotic ubiquitination.

This study identifies ATRN and ATRNL1 as transmembrane adapters that recruit MGRN1 to ubiquitinate and degrade MC1R and MC4R, expanding the known substrate repertoire of MGRN1.

The paper characterizes the expression and essentiality of protein clearance systems across human tissues and cell types, revealing tissue-specific regulation and a core set of stably expressed genes.

This study uses a ubiquitin replacement strategy to show K29-linked ubiquitylation regulates SUV39H1 stability and H3K9me3 levels in human cells.

The paper reports cryo-EM structures of the human 26S proteasome bound to K11/K48-branched ubiquitin chains, revealing a multivalent recognition mechanism involving new binding sites for K11 and alternating K11-K48 linkages.

This study investigates how UBR-box E3 ubiquitin ligases respond to changes in protein synthesis and skeletal muscle size, finding increased abundance and activity of these ligases under conditions of muscle growth and regeneration.

This study identifies and characterizes MS-8, a small-molecule activator of USP7, showing it activates mutant USP7 in a cellular context and impacts downstream proteins.

The paper shows UBE2J2 senses membrane lipid saturation by modulating its activity and interaction with E3 ligases, affecting ERAD ubiquitination.

The paper identifies Cdc48p as a key component of the RADAR pathway in yeast, which degrades misfolded peroxisomal receptors.

This study identifies USP9X as a mechanosensitive deubiquitinase that stabilizes YAP to enhance tumor cell invasiveness and drug resistance.

The paper identifies BAP1 as a deubiquitinase that stabilizes SPIN4 by counteracting degradation mediated by DCAF16.

This study analyzes 11 USP7 variants in Hao-Fountain syndrome, showing they affect enzyme activity, stability, and substrate recognition, with some variants responsive to an allosteric activator.

This paper shows PCMTD1, a cullin-RING ligase, recognizes L-isoaspartyl residues and targets damaged proteins for ubiquitylation and degradation.

The paper identifies the roles of Ubp2 and Ubp3 in editing polyubiquitin chains on ribosomes to maintain RQC activity.

The paper identifies a mechanism where Deltex E3 ligases modify tankyrase with a ubiquitin-MAR hybrid mark, preventing PAR formation and stabilizing tankyrase through interaction with RNF114 and RNF166.

This study identifies DUB inhibitors that enhance bacterial clearance in Salmonella infections and shows their potential as host-directed therapies against antibiotic-resistant pathogens.

This study presents the crystal structure of SspH1 and analyzes its conformational dynamics, showing it exists in an open-closed equilibrium with substrate binding modulating state distribution but not inducing major conformational changes.

This study develops D-box peptides that inhibit APC/C by binding Cdc20, showing they are more potent than Apcin and can drive protein degradation.

The paper investigates how genotype-by-environment interactions influence the ubiquitin-proteasome system activity in yeast by analyzing genetic effects across different environments and substrates.

The paper identifies SUMO E1 covalent allosteric inhibitors that modulate polyamine synthesis through the MAT2A-AdoMetDC axis and show synergistic effects with polyamine inhibitors in T47D cells.

This study shows AMPK regulates proteasome phosphorylation and prevents persistent proteasome condensates in yeast by modulating kinase-phosphatase activity.

This study identifies the structural basis of VCP-VCPIP1-p47 complex formation and demonstrates the role of VCPID in enhancing DUB activity and Golgi reassembly.

The paper presents the cryo-EM structure of the UBR4 complex, revealing its architecture and mechanism for substrate binding and ubiquitin chain extension in protein quality control.

This study creates the first complete SUMO Cell Atlas in eukaryotes, revealing how SUMO components vary spatially and are regulated during stress responses in Arabidopsis roots.

The paper analyzes the expression and DNA methylation of 20S proteasome subunits across cancers, finding cancer-type dependent survival associations and functional pathway impacts.

The paper identifies a small molecule, BRD1732, that is ubiquitinated in cells, leading to proteasome inhibition through accumulation of ubiquitin chains.

This study identifies the Hb group's interaction with the hydrophobic pocket as sufficient to induce gate opening in archaeal 20S proteasomes, revealing a mechanism for proteasome activation.