Regular ArticleLigand-Induced Polyubiquitination of Receptor Tyrosine Kinases
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2023, Journal of Biological ChemistryProteomic approaches for the profiling of ubiquitylation events and their applications in drug discovery
2021, Journal of ProteomicsCitation Excerpt :Dysregulation of ubiquitylation caused by mutation or abnormal expression of E3 ligases or DUBs is closely associated with many diseases including cancer, neurodegenerative diseases, cardiovascular diseases, metabolic syndromes, and inflammatory disorders [22–28]. Meanwhile, ubiquitylation is rapidly regulated under stimulation of a variety of signaling cues including external growth factors, oxidative stress, unfolded protein response, and DNA damage events [29–35]. Therefore, identification of the specific subset of substrates that are regulated by enzymes in the ubiquitin system or by signaling cues is critical for understanding the biological functions associated with dysregulated ubiquitylation events.
Macrophage Colony Stimulating Factor [CSF-1]
2003, The Cytokine HandbookA deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP
2000, Journal of Biological ChemistryCitation Excerpt :Several growth factor receptors such as platelet-derived growth factor receptor (PDGFR), epidermal growth factor receptor, and hepatocyte growth factor receptor are ubiquitinated upon ligand stimulation (26-28). It has been shown that proteasome inhibitors suppress degradation of PDGFR and hepatocyte growth factor receptor (28, 29), suggesting that in addition to the lysosomal pathway, the ubiquitin-proteasome pathway is involved in proteolytic degradation of growth factor receptors. Because the deletion mutant of Hbp lacking the SH3 domain shows dominant negative effects on degradation of PDGFR (5), binding partners of the SH3 domain seem to positively regulate degradation of growth factor receptors.