Access count of this item: 238
|Title:||Phosphorylation of the adaptor ASC acts as a molecular switch that controls the formation of speck-like aggregates and inflammasome activity.|
|Authors:||Hara, Hideki |
|Author's alias:||原, 英樹|
|Publisher:||Nature Publishing Group|
|Journal title:||Nature immunology|
|Abstract:||The inflammasome adaptor ASC contributes to innate immunity through the activation of caspase-1. Here we found that signaling pathways dependent on the kinases Syk and Jnk were required for the activation of caspase-1 via the ASC-dependent inflammasomes NLRP3 and AIM2. Inhibition of Syk or Jnk abolished the formation of ASC specks without affecting the interaction of ASC with NLRP3. ASC was phosphorylated during inflammasome activation in a Syk- and Jnk-dependent manner, which suggested that Syk and Jnk are upstream of ASC phosphorylation. Moreover, phosphorylation of Tyr144 in mouse ASC was critical for speck formation and caspase-1 activation. Our results suggest that phosphorylation of ASC controls inflammasome activity through the formation of ASC specks.|
|Description:||炎症応答を制御する新たな仕組みを解明 -慢性炎症や自己炎症性疾患の病態理解に貢献-. 京都大学プレスリリース. 2013-11-04.|
|Rights:||© 2013 Nature Publishing Group.|
この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。This is not the published version. Please cite only the published version.
|Appears in Collections:||Journal Articles |
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