CARD9

CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 9
The caspase recruitment domain (CARD) is a protein module that consists of 6 or 7 antiparallel alpha helices. It participates in apoptosis signaling through highly specific protein-protein homophilic interactions. CARDs induce nuclear factor kappa-B (NFKB; 164011) activity through the IKK (e.g., IKBKB; 603258) complex. CARD9, CARD10 (607209), CARD11 (607210), and CARD14 (607211) interact with BCL10 (603517) and are involved in NFKB signaling complexes. However, unlike CARD10, CARD11, and CARD14, CARD9 does not contain C-terminal membrane-associated guanylate kinase (MAGUK) domains (summary by Bertin et al., (2000, 2001)).
カスパーゼ導入ドメインは6,7個のαヘリックスよりなる。
高度に特異的なタンパク質間相互作用により、アポトーシスシグナリングに関与する。CARDはIKK複合体を介してNFkappaB活性化を促す。複数のCARDがBCL10と相互作用をもち、NFkappaBシグナリング複合体に含まれる。

B-CELL CLL/LYMPHOMA 10; BCL10

B-cell lymphomas of mucosa-associated lymphoid tissue (MALT lymphomas) are the most common form of lymphoma arising in extranodal sites, in most cases arising in the gastric mucosa (Isaacson and Spencer, 1995). Cytogenetic studies of low-grade malignant MALT lymphoma identified abnormalities of chromosome 1p22, in particular translocation t(1;14)(p22;q32), as uncommon but recurrent events (Wotherspoon et al., 1992). Willis et al. (1999) cloned a t(1;14)(p22;q32) translocation breakpoint from a case of low-grade MALT lymphoma and identified a recurrent breakpoint upstream of the promoter of a novel gene, BCL10. The BCL10 gene encodes a predicted protein of 233 amino acids and is a cellular homolog of the equine herpesvirus-2 gene (E10); both contain an amino-terminal caspase recruitment domain (CARD) homologous to that found in several apoptotic molecules. BCL10 was found to be expressed as a transcript of 4.2 kb in all normal and malignant tissues examined.