Thiostrepton interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates

Here, we report a novel mechanism of proteasome inhibition mediated by Thiostrepton (Thsp), which interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates. We identified Thsp in a cell‐based high‐throughput screen using a fluorescent reporter sensitive to degradation by...

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Veröffentlicht in:	Journal of cellular and molecular medicine 2015-09, Vol.19 (9), p.2181-2192
Hauptverfasser:	Sandu, Cristinel, Chandramouli, Nagaranjan, Glickman, Joseph Fraser, Molina, Henrik, Kuo, Chueh‐Ling, Kukushkin, Nikolay, Goldberg, Alfred L., Steller, Hermann
Format:	Artikel
Sprache:	eng
Schlagworte:	Adducts Apoptosis Biodegradation Cancer Chymotrypsin Covalence Experiments Gene expression Genes, Reporter HEK293 Cells Humans Inhibition Laboratories Lymphoma Mammals Mass spectrometry Mass spectroscopy Melanoma Models, Molecular Multiple myeloma Original Oxidative stress proteasome Proteasome 26S Proteasome Endopeptidase Complex - metabolism Proteasome inhibitors Proteasome Inhibitors - pharmacology Proteasomes Protein Binding - drug effects protein chemical modification protein degradation Protein Stability - drug effects Protein Subunits - metabolism Proteins Proteolysis - drug effects Scientific imaging Sensors Substrate Specificity - drug effects Substrates thiol Thiostrepton Thiostrepton - pharmacology Ubiquitin Ubiquitination
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