Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
RIPK1 integrates signals that drive both NF-κB activation and cell death pathways. Here Zhang et al. generate RIPK1 knock-in mice lacking a major ubiquitination site and demonstrate that this modification is important to suppress cell death during embryogenesis and inflammation postnatally.
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Main Authors: | , , , , , , , , , , , , , |
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Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2019
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Subjects: | |
Online Access: | https://doaj.org/article/7a20ff8bd8654fe78c8cee847d1dc433 |
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Summary: | RIPK1 integrates signals that drive both NF-κB activation and cell death pathways. Here Zhang et al. generate RIPK1 knock-in mice lacking a major ubiquitination site and demonstrate that this modification is important to suppress cell death during embryogenesis and inflammation postnatally. |
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