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BNIP3 は BH3 Domainと ミトコンドリア標的配列を有している: 安田元昭¹、進藤正信²、向後隆男²、中村太保¹　（¹北大・歯・歯科放射線、²北大・歯・口腔病理）

BCL-2 Interacting Protein BNIP3 Contains a BH3 Domain and a Mitochondrial Targeting Sequence : Motoaki Yasuda¹, Masanobu Shindoh², Takao Kohgo², Motoyasu Nakamura¹ (¹Dept. of Dental Radiol., ²Dept. of Oral Pathol., Hokkaido Univ. Sch. of Dent.)

Adenovirus E1B-19K and Bcl-2 proteins interact with certain pro-apoptotic proteins. A conserved domain, BH3, present in these proteins is essential for their pro-apoptotic activity and for heterodimerization with anti-apoptosis proteins. BNIP3 interacts with E1B-19K, Bcl-2, Bcl-xl, and EBV-BHRF1. BNIP3 contains a motif similar to the BH3 domain. Deletion of the BH3-like motif in BNIP3 abrogates its ability to heterodimerize with E1B-19K and BCL-xl. Substitution of the Bh3 domain of BNIP3 for the corresponding sequence of BAX functionally restores the pro-apoptotic and protein heterodimerization activities of BAX. BNIP3 exhibits adelayed celldeath activity that is partially relieved by deletion of the BH3 domain. BNIP3 surpresses the anti-apoptosis activity of Bcl-xl in a BH3-dependent manner. BNIP3 contains a C-terminal transmembrane (TM) domain similar to Bcl-2 family proteins. The TM domain of BNIP3 can functionally substitute for the TM domain of a Bcl-2 family member EBV-BHRF1. The BNIP3 TM domain exclusively targets the heterologus green fluorescent protein (GFP) to mitochondria. These results suggest that BNIP3 is a member of the BH3-containing Bcl-2 family of pro-apoptotic proteins and functions in mitochondria.