Cleavage of BNIP-2 and BNIP-XL by caspases.
Cleavage of BNIP-2 and BNIP-XL by caspases.
复制标题
半胱天冬酶裂解 BNIP-2 和 BNIP-XL。
DOI：
10.1016/j.bbrc.2007.10.018
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发表时间：
2007
影响因子：
3.1
通讯作者：
Liu,Rihe
中科院分区：
文献类型：
--
作者：
Valencia,CAlexander;Cotten,StevenW;Liu,Rihe
BNIP-2 and BNIP-XL are BCH domain-containing proteins that are implicated in programmed cell death. It has been reported that overexpression of BNIP-2 in neuroblastoma cell lines resulted in massive cell death, whereas BNIP-XL was upregulated during NGF-depletion-induced apoptosis in neuroblastoma and was involved in the regulation of differentiation, survival, and aggressiveness of tumor cells. Despite their importance in apoptosis, our understanding of BNIP-2 containing proteins is limited. In this communication, we demonstrate that both BNIP-2 and BNIP-XL are cleaved by caspases during apoptosis. Significantly, the caspase cleavage sites on BNIP-2 are located on its N-terminal EF-hand motif, while that on BNIP-XL is located upstream of the C-terminal BCH domain. Our results suggest that the caspase-mediated cleavage of BNIP-2 and BNIP-XL could result in the release of the BCH domain or smaller fragments that are crucial for their proapoptotic activities.
