当前位置: X-MOL 学术Proc. Natl. Acad. Sci. U.S.A. › 论文详情
CK1α, CK1δ, and CK1ε are necrosome components which phosphorylate serine 227 of human RIPK3 to activate necroptosis.
Proceedings of the National Academy of Sciences of the United States of America ( IF 9.412 ) Pub Date : 2020-01-13 , DOI: 10.1073/pnas.1917112117
Sarah Hanna-Addams,Shuzhen Liu,Hua Liu,She Chen,Zhigao Wang

Necroptosis is a regulated necrotic cell death pathway, mediated by a supermolecular complex called the necrosome, which contains receptor-interacting protein kinase 1 and 3 (RIPK1, RIPK3) and mixed-lineage kinase domain-like protein (MLKL). Phosphorylation of human RIPK3 at serine 227 (S227) has been shown to be required for downstream MLKL binding and necroptosis progression. Tandem immunoprecipitation of RIPK3 reveals that casein kinase 1 (CK1) family proteins associate with the necrosome upon necroptosis induction, and this interaction depends on the kinase activity of RIPK3. In addition, CK1 proteins colocalize with RIPK3 puncta during necroptosis. Importantly, CK1 proteins directly phosphorylate RIPK3 at S227 in vitro and in vivo. Loss of CK1 proteins abolishes S227 phosphorylation and blocks necroptosis. Furthermore, a RIPK3 mutant with mutations in the CK1 recognition motif fails to be phosphorylated at S227, does not bind or phosphorylate MLKL, and is unable to activate necroptosis. These results strongly suggest that CK1 proteins are necrosome components which are responsible for RIPK3-S227 phosphorylation.
更新日期:2020-01-29

 

全部期刊列表>>
物理学研究前沿热点精选期刊推荐
chemistry
自然职位线上招聘会
欢迎报名注册2020量子在线大会
化学领域亟待解决的问题
材料学研究精选新
GIANT
ACS ES&T Engineering
ACS ES&T Water
ACS Publications填问卷
屿渡论文,编辑服务
阿拉丁试剂right
南昌大学
王辉
南方科技大学
彭小水
隐藏1h前已浏览文章
课题组网站
新版X-MOL期刊搜索和高级搜索功能介绍
ACS材料视界
天合科研
x-mol收录
赵延川
李霄羽
廖矿标
朱守非
试剂库存
down
wechat
bug