IL-1 beta→Interleukin-1→NF-kappa B→NF-kappa B→JNK Mitogen-Activated Protein Kinases→JunD

• 19759850(IL-1+beta): A splice variant of ASC regulates IL-1beta release and aggregates differently from intact ASC.

  These results suggest that although the PGR domain is dispensable for procaspase-1 activation , it plays an important role in the regulation of the molecular structure and activity of ASC.

• 11967258(Interleukin-1): The PYRIN-CARD protein ASC is an activating adaptor for caspase-1.

  Consistent with these results ectopic expression of full-length ASC , but not its isolated CARD or PYRIN domain , with procaspase-1 induced activation of procaspase-1 and processing of pro-interleukin-1beta in transfected cells.

• 11278692(NF-kappa B): CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B.

  The caspase recruitment domain (CARD) is a protein-binding module that mediates the assembly of CARD-containing proteins into apoptosis and NF-kappaB signaling complexes.

• 18806265(NF-kappa B): Multiple protein domains mediate interaction between Bcl10 and MALT1.

  Previous studies have indicated that a 13-amino acid region downstream of the Bcl10 caspase recruitment domain (CARD) is responsible for interacting with the immunoglobulin-like domains of MALT1.

• 9837920(JNK Mitogen-Activated Protein Kinases): Analysis of the interaction between c-Jun and c-Jun N-terminal kinase in vivo.

  Our results suggest that JNK can be tethered passively to c-Jun in situ through multiple interacting regions and , when activated , can stimulate c-Jun phosphorylation without necessarily dissociating from its substrate.

• 15927205(JunD): Protein kinase p-JNK is correlated with the activation of AP-1 and its associated Jun family proteins in hepatocellular carcinoma.

  JNK phosphorylation may correlate with AP-1 activation and the expression of c-Jun and JunD in HCC.