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Phosphorylation of the adaptor ASC acts as a molecular switch that controls the formation of speck-like aggregates and inflammasome activity.

Nature immunology (2013-11-05)
Hideki Hara, Kohsuke Tsuchiya, Ikuo Kawamura, Rendong Fang, Eduardo Hernandez-Cuellar, Yanna Shen, Junichiro Mizuguchi, Edina Schweighoffer, Victor Tybulewicz, Masao Mitsuyama
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
L-酪氨酸, reagent grade, ≥98% (HPLC)
SAFC
L-酪氨酸
Sigma-Aldrich
L-酪氨酸, from non-animal source, meets EP, USP testing specifications, suitable for cell culture, 99.0-101.0%
Sigma-Aldrich
L-酪氨酸, BioUltra, ≥99.0% (NT)
Supelco
L-酪氨酸, Pharmaceutical Secondary Standard; Certified Reference Material
Sigma-Aldrich
L-酪氨酸, FG
Supelco
L-酪氨酸, certified reference material, TraceCERT®