Self-association regions in the CARD of Bcl-10
Many apoptotic signals are mediated by the association of proteins containing homologous domains, such as death domains (DD), death effector domains (DED), and caspase recruitment domains (CARD). Several CARD-containing proteins appear now to be directly involved in modulation of nuclear factor-kB (NF-kB)  and in the regulation of inflammatory responses and apoptosis. Among these, Bcl-10 (apoptosis regulator B-cell lymphoma 10) is one of the best studied for its correlation with MALT lymphomas [2, 3] and more recently as a downstream effector of lymphocyte antigen receptors to promote the activation of the IkappaB kinase complex leading to the phosphorylation and degradation of IkappaB . Bcl-10 has a bipartite structure consisting of an N-terminal CARD domain and a C-terminal serine-threonine rich domain acting as a regulatory unit that undergoes multiple phosphorylation by several kinases. Most activities of Bcl-10 are accomplished by a dimeric form of the protein;...
KeywordsMalt Lymphoma Longe Fragment Death Effector Domain Caspase Recruitment Domain Card Domain
The support of project FIRB RBNE03PX83_005 is acknowledged.