SUMO chain-induced dimerization activates RNF4 [PDF]
, 2014 Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is primed for catalysis.
Alejandro Rojas-Fernandez +64 more
core +3 more sources
Genome-Wide Identification and Expression of Xenopus F-Box Family of Proteins. [PDF]
PLoS ONE, 2015 Protein degradation via the multistep ubiquitin/26S proteasome pathway is a rapid way to alter the protein profile and drive cell processes and developmental changes.
Banu Saritas-Yildirim +3 more
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
Reciprocal control of viral infection and phosphoinositide dynamics
FEBS Letters, EarlyView.Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley +1 more source
Coupled monoubiquitylation of the co-E3 ligase DCNL1 by Ariadne RBR E3 ubiquitin ligases promotes cullin-RING ligase complex remodeling [PDF]
, 2019 Cullin-RING E3 ubiquitin ligases (CRLs) are large and diverse multisubunit protein complexes that contribute to about one-fifth of ubiquitin-dependent protein turnover in cells.
Alpi, Arno F. +5 more
core +2 more sources
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
Parkin-independent mitophagy controls chemotherapeutic response in cancer cells [PDF]
, 2017 Mitophagy is an evolutionarily conserved process that selectively targets impaired mitochondria for degradation. Defects in mitophagy are often associated with diverse pathologies, including cancer.
Bossowski, Jozef P. +13 more
core +2 more sources
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
A quantitative assay to monitor HSV-1 ICP0 ubiquitin ligase activity in vitro [PDF]
, 2015 The ubiquitin–proteasome system is an essential cellular process that plays a fundamental role in the regulation of protein stability. This pathway is tightly controlled by a sequential cascade of enzymatic steps that culminates in the formation of a ...
Boutell, Chris, Davido, David J.
core +2 more sources
The ubiquitin ligase RNF115 is required for the clearance of damaged lysosomes
FEBS Letters, EarlyView.Upon lysosomal rupture, an E3 ubiquitin ligase RNF115 translocates from the cytosol to the damaged lysosomal membrane. Moreover, RNF115 depletion impairs the clearance of damaged lysosomes, identifying it as a key regulator of lysosomal quality control.
Sae Nakanaga +3 more
wiley +1 more source