Results 111 to 120 of about 67,820 (304)
Genome-wide analysis of the U-box E3 ubiquitin ligase enzyme gene family in tomato
E3 ubiquitin ligases are a central modifier of plant signaling pathways that act through targeting proteins to the degradation pathway. U-box E3 ubiquitin ligases are a distinct class of E3 ligases that utilize intramolecular interactions for its ...
Bhaskar Sharma, Joemar Taganna
doaj +1 more source
USP15 targets ALK3/BMPR1A for deubiquitylation to enhance bone morphogenetic protein signalling [PDF]
Protein kinase ALK3/BMPR1A mediates bone morphogenetic protein (BMP) signalling through phosphorylation and activation of SMADs 1/5/8. SMAD6, a transcriptional target of BMP, negatively regulates the BMP pathway by recruiting E3 ubiquitin ligases and ...
Al-Salihi, Mazin A. +11 more
core +3 more sources
Endocytic Control of Cell‐Autonomous and Non‐Cell‐Autonomous Functions of p53
NUMB Ex3‐containing isoforms localize to the plasma membrane, where they recruit p53 through SNX9 and direct it to multivesicular bodies and exosomes. Exported p53 is taken up by neighboring cells and activates nuclear programs, revealing an intercellular, exosome‐based pathway that might help establish a tumor‐suppressive microenvironment.
Roberta Cacciatore +20 more
wiley +1 more source
Regulation of endoplasmic reticulum-associated protein degradation (ERAD) by ubiquitin [PDF]
Quality control of protein folding inside the endoplasmic reticulum (ER) includes chaperone-mediated assistance in folding and the selective targeting of terminally misfolded species to a pathway called ER-associated protein degradation, or simply ERAD.
Goder, Veit, Lemus Rodríguez,Leticia
core +2 more sources
DCAF13 Safeguards Hematopoietic Stem Cells via RRS1‐Regulated Ribosome Biogenesis
This study establishes DCAF13 as an essential regulator for hematopoietic stem cell (HSC) function. Its deletion in mice causes lethal pancytopenia and HSC depletion. Mechanistically, DCAF13 interacts with RRS1 and mediates its non‐degradative K27‐linked ubiquitination, thereby stabilizing RRS1 to maintain ribosome biogenesis and protein translation ...
Mengke Li +25 more
wiley +1 more source
Ubiquitination accomplished: E1 and E2 enzymes were not necessary [PDF]
Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 ...
Huang, Danny T., Nakasone, Mark
core +1 more source
Elevated exogenous palmitic acid promotes the S‐palmitoylation of SRPK1 in endothelial cells, a dynamic process governed by ZDHHC24 and APT1. This post‐translational modification strengthens the interaction between SRPK1 and the E3 ubiquitin ligase MIB1, thereby facilitating the proteasomal degradation of SRPK1.
Xiao‐Hui Tan +11 more
wiley +1 more source
The Ubiquitin-Proteasome System (UPS) is a key mechanism of cellular homeostasis. A central part of this mechanism is E3 ubiquitin ligases, which selectively direct proteins to be ubiquitinated for degradation via the UPS.
Srineevas Sriram +2 more
doaj +1 more source
Proteasome Lid Bridges Mitochondrial Stress with Cdc53/Cullin1 NEDDylation Status [PDF]
Cycles of Cdc53/Cullin1 rubylation (a.k.a NEDDylation) protect ubiquitin-E3 SCF (Skp1-Cullin1-F-box protein) complexes from self-destruction and play an important role in mediating the ubiquitination of key protein substrates involved in cell cycle ...
Bramasole, L. +14 more
core +1 more source
Ufmylation‐Deficient DDRGK1 Ameliorates Obesity by Inhibiting FASN‐Mediated Adipocyte Lipogenesis
DDRGK1 regulates de novo lipogenesis via stabilization of fatty acid synthase (FASN). DDRGK1‐mediated UFMylation of FASN prevents its ubiquitin–proteasomal degradation. Reduced DDRGK1 expression or mutation at the key UFMylation site enhances FASN degradation and suppresses fatty acid synthesis (FAS), resulting in smaller adipocytes and improved ...
Yin Li +16 more
wiley +1 more source

