CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM.
CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM.
复制标题
CKIP-1 通过与 ATM 相互作用将部分核 ATM 募集到质膜上。
DOI：
10.1016/j.cellsig.2005.10.017
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发表时间：
2006-09
影响因子：
4.8
通讯作者：
张令强
中科院分区：
文献类型：
--
作者：
张令强
CKIP-1(酪蛋白激酶-2相互作用蛋白-1)与肌肉分化、细胞形态调节和肌动蛋白细胞骨架有关。最近，我们发现CKIP-1通过caspase-3依赖的切割和易位来调节AP-1的活性并促进细胞凋亡。在此，我们报道了在SK-BR-3乳腺癌细胞中过表达CKIP-1可以通过增加P53 N末端Ser-15的磷酸化水平来阻止放线菌酮诱导的P53降解。CKIP-1可与P53上游的ATM相互作用，从而增强P53的稳定性。有趣的是，CKIP-1既定位于细胞膜，又定位于细胞核，这取决于细胞类型，只有定位于质膜的CKIP-1才能与ATM形成复合体。重要的是，CKIP-1将核ATM蛋白部分招募到质膜上。我们的研究结果首次证明了CKIP-1可以将以核为主的ATM重新定位到细胞膜上，并为多功能CKIP-1的研究提供了新的线索。
CKIP-1 (casein kinase-2 interacting protein-1) is implicated in muscle differentiation, regulation of cell morphology and actin cytoskeleton. More recently, we showed that CKIP-1 regulated AP-1 activity and promoted apoptosis via caspase-3-dependent cleavage and translocation. Here, we report that overexpression of CKIP-1 in SK-BR-3 breast cancer cells prevents p53 degradation induced by cycloheximide treatment through increase of p53 N-terminal Ser-15 phosphorylation level. CKIP-1 could interact with ATM, which is an upstream kinase of p53, thereby enhance the stability of p53. Interestingly, CKIP-1 is localized both at the plasma membrane and in the nucleus dependent on the cell types, and only the plasma membrane-localized CKIP-1 could form a complex with ATM. Importantly, CKIP-1 recruits nuclear ATM proteins partially to the plasma membrane. Our data provide the first evidence that ATM, a predominantly nuclear kinase, could be relocalized to the plasma membrane by CKIP-1 and shed new light on the multi-functional CKIP-1.
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影响因子：
56.9
作者：
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通讯作者：
Elledge, SJ
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影响因子：
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