Oligomerization of BCL10 and MALT1

BCL10 and MALT1 proteins form high molecular weight oligomers and only these oligomeric forms can activate IKK in vitro (Sun et al. 2004). BCL10 proteins form homo-oligomers through CARD-CARD interactions whereas in MALT1 the tandem Ig-like domains naturally form oligomers with a tendency towards dimers and tetramers (Dong et al. 2006, Quiu & Dhe-Paganon 2011). These CBM oligomers provides the molecular platform, which can facilitate dimerization or serve as scaffolds on which proteases and kinases involved in NF-kB activation are assembled and activated.

BCL10与MALT1蛋白形成高分子量寡聚体，且仅这些寡聚形态能够体外激活IKK（Sun等，2004年）。BCL10蛋白通过CARD-CARD相互作用形成同源寡聚体，而MALT1中的串联Ig样结构域自然形成寡聚体，倾向于形成二聚体和四聚体（Dong等，2006年，Qiu与Dhe-Paganon，2011年）。这些CBM寡聚体提供了分子平台，该平台可促进二聚化或作为组装和激活参与NF-kB激活的蛋白酶和激酶的支架。