High impact information on BCL2L13

• Thus, Bcl-rambo constitutes a novel type of pro-apoptotic Bcl-2 member that triggers cell death independently of its BH motifs [1].
• In mammalian cells, Bcl-rambo was localized to mitochondria, and its overexpression induces apoptosis that is specifically blocked by the caspase inhibitors, IAPs, whereas inhibitors controlling upstream events of either the 'death receptor' (FLIP, FADD-DN) or the 'mitochondrial' pro-apoptotic pathway (Bcl-x(L)) had no effect [1].
• Bcl-rambo, a novel Bcl-2 homologue that induces apoptosis via its unique C-terminal extension [1].
• No interaction of Bcl-rambo with either anti-apoptotic (Bcl-2, Bcl-x(L), Bcl-w, A1, MCL-1, E1B-19K, and BHRF1) or pro-apoptotic (Bax, Bak, Bik, Bid, Bim, and Bad) members of the Bcl-2 family was observed [1].
• Here, we report the presence of a special splicing variant of a proapoptotic protein Bcl-rambo in human lymph node, designated as Bcl-rambo beta [2].

Anatomical context of BCL2L13

• Bcl-rambo beta is detected in several adult human tissues such as heart, lymph node and cervix but is absent in human brain tissue [2].

Associations of BCL2L13 with chemical compounds

• Unlike the Bcl-rambo, Bcl-rambo beta is lacking of the BH1, BH2 and BH3 motifs and becomes a BH4-only protein [2].

References