A CONSERVED DOMAIN IN BAK, DISTINCT FROM BH1 AND BH2, MEDIATES CELL-DEATH AND PROTEIN-BINDING FUNCTIONS
A CONSERVED DOMAIN IN BAK, DISTINCT FROM BH1 AND BH2, MEDIATES CELL-DEATH AND PROTEIN-BINDING FUNCTIONS
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DOI：
10.1002/j.1460-2075.1995.tb00246.x
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发表时间：
1995-11-15
期刊：
影响因子：
11.4
通讯作者：
LUTZ, RJ
中科院分区：
文献类型：
--
作者：
CHITTENDEN, T;FLEMINGTON, C;LUTZ, RJ
细胞死亡程序的调节涉及Bcl-2家族不同成员之间的物理相互作用，其促进或抑制细胞凋亡。Bcl-2同系物巴克促进细胞凋亡并结合抗细胞凋亡家族成员，包括Bcl-2和Bcl-x（L）。我们已经鉴定了巴克中的一个结构域，该结构域对于细胞毒性活性和与Bcl-x（L）的结合是必要的和充分的。在Bar和Bip 1中鉴定出与该结构域相似的序列，这两种蛋白质促进细胞凋亡并与Bcl-x（L）相互作用，并且对于它们杀死细胞和结合Bcl-x（L）的能力同样至关重要。因此，该结构域在介导与Bcl-2家族成员相互作用的多种细胞死亡调节蛋白的功能中具有核心重要性。
Regulation of the cell death program involves physical interactions between different members of the Bcl-2 family that either promote or suppress apoptosis, The Bcl-2 homolog, Bak, promotes apoptosis and binds anti-apoptotic family members including Bcl-2 and Bcl-x(L). We have identified a domain in Bak that is both necessary and sufficient for cytotoxic activity and binding to Bcl-x(L). Sequences similar to this domain were identified in Bar and Bip1, two other proteins that promote apoptosis and interact with Bcl-x(L), and were likewise critical for their capacity to kill cells and bind Bcl-x(L). Thus, the domain is of central importance in mediating the function of multiple cell death-regulatory proteins that interact with Bcl-2 family members.