Programmed cell death 6 (PDCD6) protein interacts with death-associated protein kinase 1 (DAPk1): additive effect on apoptosis via caspase-3 dependent pathway
Programmed cell death 6 (PDCD6) protein interacts with death-associated protein kinase 1 (DAPk1): additive effect on apoptosis via caspase-3 dependent pathway
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DOI：
10.1007/s10529-005-7869-x
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发表时间：
2005-07-01
影响因子：
2.7
通讯作者：
Chun, T
中科院分区：
文献类型：
--
作者：
Lee, JH;Rho, SB;Chun, T
程序性细胞死亡6（PDCD 6）蛋白是一种22 kDa EF-手型钙离子结合蛋白，参与细胞凋亡。为了明确PDCD 6在细胞凋亡通路中的调控机制，我们利用酵母双杂交系统从人卵巢cDNA文库中寻找一种新的PDCD 6结合蛋白。选择的蛋白质是人死亡相关蛋白激酶1（DAPk 1），另一种蛋白质，作为细胞凋亡的正介导剂。PDCD 6和DAPk 1共转染肿瘤细胞系通过caspase-3依赖的途径促进凋亡。
Programmed cell death 6 (PDCD6) protein is a 22 kDa EF-hand type Ca2+-binding protein involved in apoptosis. To define the regulating mechanism of PDCD6 activity in the apoptotic pathway, we searched a human ovary cDNA library for a novel PDCD6 binding protein using a yeast two-hybrid system. The selected protein was the human death-associated protein kinase 1 (DAPk1), another protein that functions as a positive mediator of apoptosis. Co-transfection of PDCD6 and DAPk1 cDNA into a tumor cell line accelerated apoptosis via caspase-3 dependent pathway.