Methods to Discover and Evaluate Proteasome Small Molecule Stimulators
Protein accumulation has been identified as a characteristic of many degenerative conditions, such as neurodegenerative diseases and aging. In most cases, these conditions also present with diminished protein degradation. The ubiquitin-proteasome system (
Rachel A. Coleman, Darci J. Trader
doaj +1 more source
Ubiquitin-Dependent and Independent Proteasomal Degradation in Host-Pathogen Interactions
Ubiquitin, a small protein, is well known for tagging target proteins through a cascade of enzymatic reactions that lead to protein degradation. The ubiquitin tag, apart from its signaling role, is paramount in destabilizing the modified protein.
Wojciech Bialek +2 more
doaj +1 more source
Oncogenic DMTF1β promotes cancer cell motility by regulating autophagy through ULK1 stabilization
In the current study, we demonstrate that the oncogene DMTF1β regulates ULK1 stability by reducing its proteasomal degradation in cancer cells. This stabilization enables ULK1 to induce autophagy, which in turn facilitates cancer cell migration. Consequently, reduced DMTF1β levels lead to decreased autophagy and impaired cancer cell migration.
Jun Xu +13 more
wiley +1 more source
Regulation of Arabidopsis thaliana Calcineurin B-like Interacting Protein Kinases (CIPKs) by the Ubiquitin-Proteasome System [PDF]
Ubiquitin Proteasome System (UPS) regulates the abundance of proteins by first attaching ubiquitin molecules and then targeting the modified protein for degradation by the 26S proteasome.
Alotaibi, Dalal
core
This study explores the feasibility of expressing the antitumoral protein Amblyomin‐X through a suicide gene therapy approach and investigates its intracellular fate after gene delivery. Although the gene is efficiently expressed, melanoma cells rapidly degrade the Amblyomin‐X protein via proteasome activity.
Victor Dal Posolo Cinel +4 more
wiley +1 more source
Ubiquitin, ubiquitination and the ubiquitin-proteasome system in cancer [PDF]
Deep insight on Ubiquitin, ubiquitination and the ubiquitin-proteasome system in ...
Voutsadakis, IA, IA Voutsadakis
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Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators [PDF]
The ubiquitin-proteasome system is vital to hormone-mediated developmental and stress responses in plants. Ubiquitin ligases target hormone-specific transcriptional activators (TAs) for degradation, but how TAs are processed by proteasomes remains ...
Grey, Heather +11 more
core +1 more source
The ubiquitin-proteasome system in glioma cell cycle control
A major determinant of cell fate is regulation of cell cycle. Tight regulation of this process is lost during the course of development and progression of various tumors.
Vlachostergios Panagiotis J +2 more
doaj +1 more source
Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. [PDF]
The specific and covalent addition of ubiquitin to proteins, known as ubiquitination, is a eukaryotic-specific modification central to many cellular processes, such as cell cycle progression, transcriptional regulation, and hormone signaling ...
Aurélie Angot +3 more
doaj +1 more source
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane +11 more
wiley +1 more source

