HECT ubiquitin ligases as accessory proteins of the plant proteasome [PDF]
The proteasome plays vital roles in eukaryotic cells by orchestrating the regulated degradation of large repertoires of substrates involved in numerous biological processes.
Wang, Zhishuo +2 more
core +1 more source
The enigma of the RING-UIM E3 ligases: its transformative impact on cancer research
RING-UIM E3 ligases, a subfamily within the RING-type E3 ligases, comprise four members: RNF114, RNF125, RNF138, and RNF166. These ligases are crucial in various biological processes, including immunity, inflammation, epigenetics, and homologous ...
Ye Wang, Yue Zhao, Qi Xin, Jihong Zhang
doaj +1 more source
Characterization of the tubulin-tyrosine ligase. [PDF]
The sequence of tubulin-tyrosine ligase (TTL), the enzyme catalyzing the ATP-dependent posttranslational addition of a tyrosine to the carboxyterminal end of detyrosinated alpha-tubulin, has been determined. TTL from bovine and porcine brain was purified by immunoaffinity chromatography and extensively characterized by protein sequencing ...
Ersfeld, K. +5 more
openaire +4 more sources
Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?
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
A Bacterial Platform for Studying Ubiquitination Cascades Anchored by SCF-Type E3 Ubiquitin Ligases
Ubiquitination is one of the most important post-translational modifications in eukaryotes. The ubiquitination cascade includes ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The E3 ligases, responsible
Zuo-Xian Pu +9 more
doaj +1 more source
A screen for E3 ubiquitination ligases that genetically interact with the adaptor protein Cindr during Drosophila eye patterning. [PDF]
Ubiquitination is a crucial post-translational modification that can target proteins for degradation. The E3 ubiquitin ligases are responsible for recognizing substrate proteins for ubiquitination, hence providing specificity to the process of protein ...
Kwami F Ketosugbo +2 more
doaj +1 more source
Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation
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
Cullin 3 ubiquitin ligases in cancer biology: functions and therapeutic implications
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
Female breast cancer has become the most commonly occurring cancer worldwide. Although it has a good prognosis under early diagnosis and appropriate treatment, breast cancer metastasis drastically causes mortality.
Yingshuang Wang +8 more
doaj +1 more source
Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz +11 more
wiley +1 more source

