期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 279, 期 12, 页码 11503-11512出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M311922200
关键词
-
p21(Bax) is a pro-apoptotic member of the Bcl-2 family and is converted by calpain into a truncated form called p18(Bax). This proteolysis enhanced the apoptogenic properties of Bax by a mechanism not yet elucidated. We have shown recently that the first alpha helix (Halpha1) of p21(Bax) contained a mitochondrial addressing sequence, which appeared to be necessary for p21(Bax)-induced apoptosis (Cartron, P. F., Priault, M., Oliver, L., Meflah, K., Manon, S., and Vallette, F. M. (2003) J. Biol. Chem. 278, 11633 11641). This feature is in contradiction with the high apoptogenic profile of p18(Bax), because the Halpha1 is lost during the calpain cleavage of p21(Bax). We investigated the role of p18(Bax) in apoptosis and found that its activity required the presence of p21(Bax). In addition, p18(Bax) exhibited a higher affinity for Bcl-Xl than p21(Bax) did, a property that seems to be essential for the fulfillment of its pro-apoptotic role. In conclusion, calpain proteolysis converts the multi-domain p21(Bax) into a Bcl-2 homology 3-like protein capable of overcoming the inhibition of apoptosis due to Bcl-Xl.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据