Identifying the ubiquitination targets of E6AP by orthogonal ubiquitin transfer

E3 ubiquitin ligases regulate biological functions by ubiquitinating defined substrate proteins but overlapping specificities complicate the identification of E3-substrate relationships. Here, the authors construct an orthogonal UB transfer cascade and identify specific substrates of the E3 enzyme E...

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Autores principales: Yiyang Wang, Xianpeng Liu, Li Zhou, Duc Duong, Karan Bhuripanyo, Bo Zhao, Han Zhou, Ruochuan Liu, Yingtao Bi, Hiroaki Kiyokawa, Jun Yin
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/618a294ce3c64f68ae20e405e16ee8b0
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Sumario:E3 ubiquitin ligases regulate biological functions by ubiquitinating defined substrate proteins but overlapping specificities complicate the identification of E3-substrate relationships. Here, the authors construct an orthogonal UB transfer cascade and identify specific substrates of the E3 enzyme E6AP.