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首页> 外文期刊>Cellular Signalling >The mammalian STE20-like kinase 1 (MST1) is a substrate for the apoptosis inhibiting protein kinase CK2
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The mammalian STE20-like kinase 1 (MST1) is a substrate for the apoptosis inhibiting protein kinase CK2

机译：哺乳动物STE20样激酶1（MST1）是凋亡抑制蛋白激酶CK2的底物

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摘要

Apoptosis and the response to cell stress are evolutionary highly conserved mechanisms. Both processes require strict regulation, which is often performed by protein kinases. The mammalian Sterile 20-like kinase 1 (MST1) is a pro-apoptotic protein kinase, which is activated and cleaved by caspases upon the induction of cell stress. Being a phosphoprotein itself, the activity of MST1 is regulated by phosphorylation. Protein kinase CK2 is an anti-apoptotic protein kinase which seems to be involved in the regulation of many different cellular processes including apoptosis. There is increasing evidence that the cleavage of many substrates by caspases is regulated by phosphorylation in the close vicinity of the caspase cleavage sites. One of these kinases, implicated in the phosphorylation of caspase substrates, is protein kinase CK2. Here, we report that serine 320 of the MST1 protein is a novel phosphorylation site for the anti-apoptotic protein kinase CK2. Although serine 320 is in close vicinity to the caspase 3 cleavage site, caspase 3 cleavage of MST1 is not affected by CK2 phosphorylation. Using biochemical approaches, we were able to show that MST1 co-localizes with the CK2 subunits in the pancreatic beta-cell line INS-1 and that full-length MST1 and the activated N-terminal fragment of MST1 both interacted with the CK2 subunits in vitro and in vivo. MST1 is a basophilic kinase whereas CK2 is an acidophilic kinase. Thus, binding of these two kinases in the cytosol and in the nucleus opens the door to the phosphorylation of a variety of new substrates.
机译：细胞凋亡和对细胞应激的反应是高度保守的进化机制。这两个过程都需要严格的调控，通常由蛋白激酶来完成。哺乳动物无菌类20激酶1（MST1）是一种促凋亡蛋白激酶，在细胞应激诱导下被半胱天冬酶激活和切割。作为一种磷蛋白，MST1的活性受磷酸化调节。蛋白激酶CK2是一种抗凋亡蛋白激酶，似乎参与了包括凋亡在内的许多不同细胞过程的调节。越来越多的证据表明，许多底物被半胱天冬酶切割是由半胱天冬酶切割位点附近的磷酸化调节的。其中一种与半胱天冬酶底物的磷酸化有关的激酶是蛋白激酶CK2。在这里，我们报道了MST1蛋白的丝氨酸320是抗凋亡蛋白激酶CK2的一个新的磷酸化位点。尽管丝氨酸320靠近半胱天冬酶3裂解位点，但MST1的半胱天冬酶3裂解不受CK2磷酸化的影响。利用生物化学方法，我们能够证明MST1与胰腺β细胞系INS-1中的CK2亚单位共定位，并且全长MST1和MST1的活化N端片段在体外和体内都与CK2亚单位相互作用。MST1是一种嗜碱性激酶，而CK2是一种嗜酸性激酶。因此，细胞质和细胞核中这两种激酶的结合为多种新底物的磷酸化打开了大门。

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