The Role of Bcl-2 Family Proteins in Therapy Responses of Malignant Astrocytic Gliomas: Bcl2L12 and Beyond
Figure 1
The Bcl-2 family. Domain structure of mammalian, viral, and C. elegans proteins. Shown are antiapoptotic “core” proteins, atypical Bcl-2-like proteins, for example, Bcl2L12 and Bcl2L13, proapoptotic multidomain, and BH3-only proteins. Bcl2L12 is characterized by six PxxP motifs located in the N-terminal and center portion of the molecule; these PxxP motifs are depicted as dark red boxes. BH: Bcl-2 homology domain; BHNo: no BH domain; TM: transmembrane domain. Bcl-2: B-cell lymphoma-2; Mcl-1: myeloid cell leukemia sequence 1 (Bcl-2-related); Bim: Bcl-2-interacting mediator of cell death; Bad: Bcl-xL/Bcl-2-associated death promoter; Bid: Bcl-2-interacting domain; Puma: p53 upregulated mediator of apoptosis; Bik: Bcl-2-interacting killer; Bmf: Bcl-2-modifying factor; Hrk: Harakiri; Bcl2Lxx: Bcl-2-Like xx; Bok: Bcl-2-related ovarian killer protein; ORF: open reading frame; Bax: Bcl-2-associated X protein; Bak: Bcl-2-antagonist/killer 1; CED-9: cell death abnormality family member; Bnip3: Bcl-2/adenovirus E1B 19 kDa interacting protein 3; Egl-1: egg laying abnormal-1; Mule: Mcl-1 ubiquitin ligase E3. Size of proteins is only approximate.
