Results 51 to 60 of about 254,188 (362)
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
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
Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10
FEBS Letters, EarlyView.Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang +8 more
wiley +1 more source
Phosphorylation of Arabidopsis SINA2 by CDKG1 affects its ubiquitin ligase activity
BMC Plant Biology, 2018 Background SEVEN IN ABSENTIA (SINA) is a RING domain-containing ubiquitin ligase involved in Drosophila eye formation. SINA-like proteins in plants are involved in several signaling pathways.
Yang Chen +5 more
doaj +1 more source
Nature Structural &Molecular Biology, 2017 RING-between-RING (RBR) E3 ligases are a class of ubiquitin ligases distinct from RING or HECT E3 ligases. An important RBR ligase is Parkin, mutations in which lead to early-onset hereditary Parkinsonism.
Atul Kumar +9 more
semanticscholar +1 more source
Prion, 2012 Failure to eliminate abnormal proteins in the cell is associated with numerous aggregation diseases. Misfolded proteins are normally detected by protein quality control and either refolded or eliminated. The ubiquitin-proteasome system is a major pathway that degrades these unwanted proteins.
Nancy N, Fang, Thibault, Mayor
openaire +2 more sources
Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing
FEBS Letters, EarlyView.Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley +1 more source
Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation
FEBS Letters, EarlyView.Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe +3 more
wiley +1 more source
MG53/TRIM72: multi-organ repair protein and beyond
Frontiers in PhysiologyMG53, a member of the tripartite motif protein family, possesses multiple functionalities due to its classic membrane repair function, anti-inflammatory ability, and E3 ubiquitin ligase properties.
Yong-Fei Wang +9 more
doaj +1 more source
The linear ubiquitin chain assembly complex (LUBAC) generates heterotypic ubiquitin chains
eLife, 2021 The linear ubiquitin chain assembly complex (LUBAC) is the only known ubiquitin ligase for linear/Met1-linked ubiquitin chain formation. One of the LUBAC components, heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1L), was recently shown to catalyse oxyester
Alan Rodriguez Carvajal +14 more
doaj +1 more source