Ubiquitin and proteasome pathways

This study identifies THAP1 as a regulator of PSMB5 expression, showing that its loss impairs proteasome function and contributes to dystonia.

This study identifies how VCP interacts with DUBs at distinct sites to coordinate ubiquitin removal during protein recycling.

This paper develops a fast, sensitive assay for measuring UBE3A ubiquitin ligase activity using fluorescence detection, suitable for preclinical and clinical applications.

This study identifies Ubp1 as a PCNA deubiquitylase that cooperates with Ubp10 and Ubp12 to regulate DNA replication by controlling PCNA ubiquitylation at replication forks.

The paper identifies two cooperating motifs in Roq1 that modulate Ubr1 activity, enhancing ubiquitination of both folded and misfolded proteins during proteotoxic stress.

The study identifies interacting proteins of TARANI/UBIQUITIN SPECIFIC PROTEASE-14 in Arabidopsis thaliana using immunoprecipitation mass spectrometry and other methods, revealing 92 interactors involved in various biological processes.

The paper shows that K63 ubiquitin chains accumulate in non-cytosolic compartments during oxidative stress and that VCP/p97 and NPLOC4 regulate their localization and removal.

The paper identifies the UBR4-KCMF1 ubiquitin ligase complex as a convergence point for quality control pathways that degrade orphan subunits, highlighting its role in protein homeostasis and cancer vulnerability.

This paper identifies Insomniac as a Cul3 adaptor protein that regulates sleep and synaptic homeostasis in Drosophila, linking Cul3 dysfunction to autism and schizophrenia.

The paper develops activity-based probes to selectively detect USP18 activity and screen for inhibitors, enabling analysis of USP18's role in disease states.

This study presents cryo-EM structures of the Bag1-bound 26S proteasome, revealing a mechanism for ubiquitin-independent proteasomal degradation through conformational changes in the 19S regulatory particle.

This study identifies SHKBP1 as a regulator of p62 oligomerization and antioxidant response by preventing Keap1 sequestration into p62 bodies, independent of ubiquitination.

The paper quantifies proteasome re-organization during proteotoxic stress using single-molecule microscopy and shows cytoskeleton-dependent movement restrictions.

This study investigates the structural dynamics of USP30 inhibition by a covalent inhibitor, revealing its binding mechanism and selectivity advantages over non-covalent inhibitors.

The paper shows that loss of 19S proteasome subunits causes monopolar spindles by ubiquitin-independent degradation of KIF11, highlighting a non-canonical role for the proteasome in mitosis.

This study develops a reaction-diffusion model to quantify proteasome-associated liquid-liquid phase separation and its bidirectional impact on degradation efficiency.

The paper investigates C-terminal cyclic imides as protein damage products, their formation mechanisms, and their impact on protein stability and quality control via CRBN.

This study identifies PHD2 interaction hotspots and reveals its role in regulating protein neddylation through interaction with the COP9 Signalosome complex.

The paper describes a method to incorporate a photo-crosslinkable amino acid into the 26S proteasome base subcomplex using recombinant expression in E. coli.

The paper identifies FBXO21 as a therapeutic target in AML by developing a small molecule that inhibits p85 ubiquitination, reducing PI3K pathway activity and inducing cell death.

This study identifies UBE3C and NRF1-dependent proteasomal pathways that regulate acute protein aggregate turnover in response to misfolded protein accumulation.

The paper identifies PITHD1 as an endogenous inhibitor of the 26S proteasome in dormant cells, revealing a triple-lock mechanism that prevents protein degradation during cellular dormancy.

The paper investigates protein quality control (PQC) in quiescent yeast cells, showing that degradation pathways like proteasomes, autophagy, and nucleus-vacuole junctions are active and required for misfolded protein clearance.

The paper identifies CoaX, a pseudokinase, and pantothenate as regulators of proteasomal degradation of the pantothenate synthesis enzyme PanB in M. tuberculosis.

This study identifies USP53 and USP54 as active deubiquitinases specific for K63-linked polyubiquitin, revealing their role in regulating tricellular junctions and correcting previous annotations of them as pseudo-enzymes.

This study identifies structural diversity and Ca2+-mediated oligomerization in bacterial ubiquitin-like proteins, suggesting a role in stress response.

This study identifies USP7 as a regulator of cell-cell adhesion in colorectal cancer through its interaction with Ajuba, showing reduced adhesion upon USP7 or Ajuba knockdown.

This study uses cryo-EM and genetic engineering to show how USP14 non-catalytically regulates proteasome activity through salt-dependent allosteric changes.

The paper determines the cryo-EM structure of the UBA7-UBE2L6 disulfide complex and identifies factors influencing its formation, revealing its role in ISG15 conjugation and immune response regulation.