The C-terminal tail of protein kinase D2 and protein kinase D3 regulates their intracellular distribution
The C-terminal tail of protein kinase D2 and protein kinase D3 regulates their intracellular distribution
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DOI：
10.1016/j.bbrc.2006.02.013
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发表时间：
2006-04-14
影响因子：
3.1
通讯作者：
Rey, O
中科院分区：
文献类型：
--
作者：
Papazyan, R;Rozengurt, E;Rey, O
我们在蛋白激酶 D2 (PKD2) 和蛋白激酶 D3 (PKD3) 之间生成了一组 GFP 标记的嵌合体，以在活细胞中检查其 C 末端区域对其细胞内定位的贡献。我们发现，当 PYD2 和 PKD3 的催化结构域在没有其他激酶结构域的情况下表达时，可以定位于细胞核。然而，当 PKD2 的 C 末端尾部添加到其催化结构域时，所得蛋白质的核定位受到抑制。相反，PKD3 CID 的核定位不受其 C 末端尾部的抑制。此外，全长蛋白中 PKD2 和 PKD3 C 端尾部的交换足以交换它们的细胞内定位。总的来说，这些数据表明这些激酶的短 C 端尾在确定其细胞质/核定位中起着关键作用。 (c) 2006 Elsevier Inc. 保留所有权利。
We generated a set of GFP-tagged chimeras between protein kinase D2 (PKD2) and protein kinase D3 (PKD3) to examine in live cells the contribution of their C-terminal region to their intracellular localization. We found that the catalytic domain of PYD2 and PKD3 can localize to the nucleus when expressed without other kinase domains. However, when the C-terminal tail of PKD2 was added to its catalytic domain, the nuclear localization of the resulting protein was inhibited. In contrast, the nuclear localization of the CID of PKD3 was not inhibited by its C-terminal tail. Furthermore, the exchange of the C-terminal tail of PKD2 and PKD3 in the full-length proteins was sufficient to exchange their intracellular localization. Collectively, these data demonstrate that the short C-terminal tail of these kinases plays a critical role in determining their cytoplasmic/nuclear localization. (c) 2006 Elsevier Inc. All rights reserved.