The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating double-strand break repair [PDF]
, 2018 Double-strand breaks (DSBs) are critical DNA lesions that robustly activate the elaborate DNA damage response (DDR) network. We identified a critical player in DDR fine-tuning - the E3/E4 ubiquitin ligase, UBE4A.
Baranes Bachar, Keren +4 more
core +1 more source
Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity
Cells, 2021 Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite
Utsa Bhaduri, Giuseppe Merla
doaj +1 more source
Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation [PDF]
, 2018 The E3 ligase parkin ubiquitinates outer mitochondrial membrane proteins during oxidative stress and is linked to early-onset Parkinson’s disease. Parkin is autoinhibited but is activated by the kinase PINK1 that phosphorylates ubiquitin leading to ...
Aguirre, Jacob D. +9 more
core +1 more source
Strategies to Target Specific Components of the Ubiquitin Conjugation/Deconjugation Machinery
Frontiers in Chemistry, 2020 The regulation of ubiquitination status in the cell is controlled by ubiquitin ligases acting in tandem with deubiquitinating enzymes. Ubiquitination controls many key processes in the cell from division to death making its tight regulation key to ...
Neil C. Taylor, Joanna F. McGouran
doaj +1 more source
Rapid degradation of mutant SLC25A46 by the ubiquitin-proteasome system results in MFN1/2-mediated hyperfusion of mitochondria. [PDF]
, 2017 SCL25A46 is a mitochondrial carrier protein that surprisingly localizes to the outer membrane and is distantly related to Ugo1. Here we show that a subset of SLC25A46 interacts with mitochondrial dynamics components and the MICOS complex.
Claypool, Steven M +6 more
core +1 more source
E3-ubiquitin ligases and recent progress in osteoimmunology
Frontiers in Immunology, 2023 Ubiquitin-mediated proteasomal degradation is a post-transcriptional protein modification that is comprised of various components including the 76-amino acid protein ubiquitin (Ub), Ub-activating enzyme (E1), Ub-conjugating enzyme (E2), ubiquitin ligase (
Yosuke Asano +8 more
doaj +1 more source
Cullin 3 ubiquitin ligases in cancer biology: functions and therapeutic implications
Frontiers in Oncology, 2016 Cullin-RING ubiquitin ligases are the largest E3 ligase family in eukaryotes and are multi-protein complexes. In these complexes, the Cullin protein serves as a scaffold to connect two functional modules of the ligases, the catalytic subunit and ...
Hsin-Yi eChen +2 more
doaj +1 more source
Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase. [PDF]
PLoS ONE, 2013 The ubiquitin-signaling pathway utilizes E1 activating, E2 conjugating, and E3 ligase enzymes to sequentially transfer the small modifier protein ubiquitin to a substrate protein.
Donald E Spratt +2 more
doaj +1 more source
A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway. [PDF]
, 2013 The endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for disposing misfolded proteins from the endoplasmic reticulum by inducing their ubiquitination and degradation.
Anania, Veronica +4 more
core +3 more sources
Role of RING-Type E3 Ubiquitin Ligases in Inflammatory Signalling and Inflammatory Bowel Disease
Mediators of Inflammation, 2020 Ubiquitination is a three-step enzymatic cascade for posttranslational protein modification. It includes the ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3).
Liguo Zhu +7 more
doaj +1 more source