Results 61 to 70 of about 349,913 (393)
The role of Schizosaccharomyces pombe SUMO ligases in genome stability [PDF]
, 2007 SUMOylation is a post-translational modification that affects a large number of proteins, many of which are nuclear. While the role of SUMOylation is beginning to be elucidated, it is clear that understanding the mechanisms that regulate the process is ...
A. Skilton +44 more
core +2 more sources
A Key Role for the Ubiquitin Ligase UBR4 in Myofiber Hypertrophy in Drosophila and Mice
Cell Reports, 2019 Summary: Skeletal muscle cell (myofiber) atrophy is a detrimental component of aging and cancer that primarily results from muscle protein degradation via the proteasome and ubiquitin ligases.
Liam C. Hunt +11 more
doaj +1 more source
Nature Communications, 2017 E3 ubiquitin ligases are key enzymes within the ubiquitin proteasome system which catalyze the ubiquitination of proteins, targeting them for proteasomal degradation.
Chiara Maniaci +8 more
semanticscholar +1 more source
PEX2 is the E3 ubiquitin ligase required for pexophagy during starvation
Journal of Cell Biology, 2016 Sargent et al. identify the E3 ubiquitin ligase PEX2 as the causative agent of mammalian pexophagy. During amino acid starvation, PEX2 expression increases to ubiquitinate peroxisomal membrane proteins and signal peroxisome degradation by autophagy.
Graeme Sargent +6 more
semanticscholar +1 more source
SUMO-targeted ubiquitin ligases
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014 Covalent posttranslational modification with SUMO (small ubiquitin-related modifier) modulates functions of a wide range of proteins in eukaryotic cells. Sumoylation affects the activity, interaction properties, subcellular localization and the stability of its substrate proteins.
Sriramachandran, Annie M. +1 more
openaire +2 more sources
Differential regulation of RNF8-mediated Lys48- and Lys63-based poly-ubiquitylation [PDF]
, 2012 Pairing of a given E3 ubiquitin ligase with different E2s allows synthesis of ubiquitin conjugates of different topologies. While this phenomenon contributes to functional diversity, it remains largely unknown how a single E3 ubiquitin ligase recognizes ...
Ching, YP +6 more
core +1 more source
Control of the SCFSkp2–Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase
Nature, 2004 Skp2 and its cofactor Cks1 are the substrate-targeting subunits of the SCF(Skp2-Cks1) (Skp1/Cul1/F-box protein) ubiquitin ligase complex that regulates entry into S phase by inducing the degradation of the cyclin-dependent kinase inhibitors p21 and p27 (ref. 1). Skp2 is an oncoprotein that often shows increased expression in human cancers; however, the
Bashir, Tarig +4 more
openaire +2 more sources
The role of fibroblast growth factors in cell and cancer metabolism
FEBS Letters, EarlyView.Fibroblast growth factor (FGF) signaling regulates crucial signaling cascades that promote cell proliferation, survival, and metabolism. Therefore, FGFs and their receptors are often dysregulated in human diseases, including cancer, to sustain proliferation and rewire metabolism.
Jessica Price, Chiara Francavilla
wiley +1 more source
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Journal of Cell Biology, 2014 PINK1 phosphorylates ubiquitin, which then binds to Parkin and activates its E3 ligase activity, leading to induction of selective autophagy of damaged mitochondria.
L. A. Kane +7 more
semanticscholar +1 more source
Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?
FEBS Letters, EarlyView.This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes +3 more
wiley +1 more source