Phosphorylation of the E3 ubiquitin protein ligase ITCH diminishes binding to its cognate E2 ubiquitin ligase

Heightened and extended inflammation underlies the pathogenesis of many disorders, including inflammatory bowel disease, sepsis, and inflammatory arthritis. Ubiquitin networks help dictate the strength and duration of inflammatory signaling. In innate immunity, the itchy E3 ubiquitin protein ligase...

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Veröffentlicht in:	The Journal of biological chemistry 2018-01, Vol.293 (3), p.1100-1105
Hauptverfasser:	Perez, Jessica M., Chen, Yinghua, Xiao, Tsan S., Abbott, Derek W.
Format:	Artikel
Sprache:	eng
Schlagworte:	E3 ubiquitin ligase HEK293 Cells Humans IKKβ Immunoprecipitation inflammation Inflammation - metabolism ITCH NF-kappa B NF-kappa B - metabolism NF-κB Phosphorylation Protein Binding Repressor Proteins - metabolism Signal Transduction UbcH7 ubiquitin ligase Ubiquitin-Protein Ligases - metabolism ubiquitination Ubiquitination - physiology
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