Article
Mutations that prevent caspase cleavage of RIPK1 cause autoinflammatory disease.
Nature - 1 Jan 2020
Lalaoui Najoua, Boyden Steven E, Oda Hirotsugu, Wood Geryl M, Stone Deborah L, Chau Diep, Liu Lin, Stoffels Monique, Kratina Tobias, Lawlor Kate E, Zaal Kristien J M, Hoffmann Patrycja M, Etemadi Nima, Shield-Artin Kristy, Biben Christine, Tsai Wanxia Li, Blake Mary D, Kuehn Hye Sun, Yang Dan, Anderton Holly, Silke Natasha, Wachsmuth Laurens, Zheng Lixin, Moura Natalia Sampaio, Beck David B, Gutierrez-Cruz Gustavo, Ombrello Amanda K, Pinto-Patarroyo Gineth P, Kueh Andrew J, Herold Marco J, Hall Cathrine, Wang Hongying, Chae Jae Jin, Dmitrieva Natalia I, McKenzie Mark, Light Amanda, Barham Beverly K, Jones Anne, Romeo Tina M, Zhou Qing, Aksentijevich Ivona, Mullikin James C, Gross Andrew J, Shum Anthony K, Hawkins Edwin D, Masters Seth L, Lenardo Michael J, Boehm Manfred, Rosenzweig Sergio D, Pasparakis Manolis, Voss Anne K, Gadina Massimo, Kastner Daniel L, Silke John
Abstract excerpt
RIPK1 is a key regulator of innate immune signalling pathways. To ensure an optimal inflammatory response, RIPK1 is regulated post-translationally by well-characterized ubiquitylation and phosphorylation events, as well as by caspase-8-mediated cleavage1-7. The physiological relevance of this cleavage event remains unclear, although it is thought to inhibit activation of RIPK3 and necroptosis8. Here we show that...
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