Epigenetic Regulation in the Pathogenesis of Renal Inflammation: Insights and Therapeutic Potentials
ABSTRACT Renal inflammation is a common pathological process in various kidney diseases, often initiated by factors such as toxins, ischemia, or autoimmune reactions. This inflammatory response can result in structural damage and a rapid decline in renal function.
Yu‐Hang Dong +5 more
wiley +1 more source
Exo70-Mediated Recruitment of Nucleoporin Nup62 at the Leading Edge of Migrating Cells is Required for Cell Migration [PDF]
Nucleoporin Nup62 localizes at the central channel of the nuclear pore complex and is essential for nucleocytoplasmic transport. Through its FG-repeat domain, Nup62 regulates nuclear pore permeability and binds nuclear transport receptors.
Bayliss +61 more
core +1 more source
N6‐Methyladenosine (m6A) in Liver Disease: Pathogenic Mechanisms and Therapeutic Potential
ABSTRACT Accumulating evidence highlights the critical role of epigenetic modifications, particularly N6‐methyladenosine (m6A), in liver disease. As the most abundant RNA modification in eukaryotic cells, m6A is dynamically regulated by multicomponent m6A methyltransferases (e.g., METTL3 and METTL14), demethylases (FTO and ALKBH5), and m6A‐binding ...
Yingfen Chen +6 more
wiley +1 more source
Human polycomb 2 protein is a SUMO E3 ligase and alleviates substrate-induced inhibition of cystathionine beta-synthase sumoylation. [PDF]
Human cystathionine beta-synthase (CBS) catalyzes the first irreversible step in the transsulfuration pathway and commits homocysteine to the synthesis of cysteine. Mutations in CBS are the most common cause of severe hereditary hyperhomocysteinemia.
Nitish Agrawal, Ruma Banerjee
doaj +1 more source
The ubiquitin system and jasmonate signaling [PDF]
The ubiquitin (Ub) system is involved in most, if not all, biological processes in eukaryotes. The major specificity determinants of this system are the E3 ligases, which bind and ubiquitinate specific sets of proteins and are thereby responsible for ...
Goossens, Alain +2 more
core +3 more sources
Extranuclear SUMOylation in Neurons [PDF]
Post-translational modification of substrate proteins by SUMO conjugation regulates a diverse array of cellular processes. While predominantly a nuclear protein modification, there is a growing appreciation that SUMOylation of proteins outside the nucleus plays direct roles in controlling synaptic transmission, neuronal excitability, and adaptive ...
Jeremy M. Henley +2 more
openaire +4 more sources
This review illustrates how scientists engineer exosomes by hijacking the cell's own cargo‐sorting machinery. These strategies efficiently load therapeutic molecules into natural vesicles, creating powerful next‐generation drug delivery systems (Created with BioGDP.com).
Huanrong Zhu +6 more
wiley +1 more source
Rhes, a Physiologic Regulator of Sumoylation, Enhances Cross-sumoylation between the Basic Sumoylation Enzymes E1 and Ubc9 [PDF]
We recently reported that the small G-protein Rhes has the properties of a SUMO-E3 ligase and mediates mutant huntingtin (mHtt) cytotoxicity. We now demonstrate that Rhes is a physiologic regulator of sumoylation, which is markedly reduced in the corpus striatum of Rhes-deleted mice.
SUBRAMANIAM SIRINIVASA +5 more
openaire +3 more sources
SUMOylation, a dynamic post‐translational modification, acts as a master regulator at the heart of tumor malignancy. Our work delineates how the SUMOylation cycle—mediated by E1/E2/E3 enzymes and reversed by SENPs—orchestrates multiple hallmarks of cancer. The central pathway converges on three critical pathological axes: 1.
Yimao Wu +6 more
wiley +1 more source
Ligand binding reduces SUMOylation of the peroxisome proliferator-activated receptor γ (PPARγ) activation function 1 (AF1) domain. [PDF]
Peroxisome proliferator-activated receptor gamma (PPARγ) is a ligand-activated nuclear receptor regulating adipogenesis, glucose homeostasis and inflammatory responses.
Rolf Diezko, Guntram Suske
doaj +1 more source

