Protein semisynthesis reveals plasticity in HECT E3 ubiquitin ligase mechanisms

Lys ubiquitination is catalysed by E3 ubiquitin ligases and is central to the regulation of protein stability and cell signalling in normal and disease states. There are gaps in our understanding of E3 mechanisms, and here we use protein semisynthesis, chemical rescue, microscale thermophoresis and...

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Veröffentlicht in:	Nature chemistry 2024-11, Vol.16 (11), p.1894-1905
Hauptverfasser:	Jiang, Hanjie, Miller, Bryant D., Viennet, Thibault, Kim, Hyojeon, Lee, Kwangwoon, Arthanari, Haribabu, Cole, Philip A.
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/173 631/92/458/582 Analytical Chemistry Biochemistry Catalysis Chemistry Chemistry and Materials Science Chemistry/Food Science Endosomal Sorting Complexes Required for Transport Inorganic Chemistry Intermediates Lysine Models, Molecular Organic Chemistry Physical Chemistry Plastic properties Plasticity Protein turnover Proteins Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Semisynthesis Stability Thermophoresis Ubiquitin - chemistry Ubiquitin - metabolism Ubiquitin-protein ligase Ubiquitin-Protein Ligase Complexes - chemistry Ubiquitin-Protein Ligase Complexes - metabolism Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - metabolism Ubiquitination Yeasts
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