Newly identified stress-responsive protein kinases, Krs-1 and Krs-2
Newly identified stress-responsive protein kinases, Krs-1 and Krs-2
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DOI：
10.1073/pnas.93.19.10099
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发表时间：
1996-09-17
影响因子：
11.1
通讯作者：
Erikson, RL
中科院分区：
文献类型：
--
作者：
Taylor, LK;Wang, HCR;Erikson, RL
蛋白激酶的激活是细胞对生长因子、化学物质、热休克或凋亡诱导剂处理的频繁反应。然而，当几种试剂导致相同酶的激活时，尚不清楚如何产生特定的生物反应。我们在这里描述了两种蛋白激酶，它们被应激条件或凋亡剂的子集激活，但不被常用的促有丝分裂刺激激活。纯化和克隆表明，这些蛋白激酶是与Ste 20 p相关的激酶亚家族的成员，Ste 20 p是一种丝氨酸/苏氨酸激酶，其在酵母中的信息素响应信号转导级联中早期起作用。Krs-1和Krs-2激活的特异性及其与Ste 20 p的相似性表明，它们可能在磷酸化事件的早期发挥作用，磷酸化事件是对某些形式的化学应激或极端热休克的特异性反应。
The activation of protein kinases is a frequent response of cells to treatment with growth factors, chemicals, heat shock, or apoptosis-inducing agents. However, when several agents result in the activation of the same enzymes, it is unclear how specific biological responses are generated. We describe here two protein kinases that are activated by a subset of stress conditions or apoptotic agents but are not activated by commonly used mitogenic stimuli. Purification and cloning demonstrate that these protein kinases are members of a subfamily of kinases related to Ste20p, a serine/threonine kinase that functions early in a pheromone responsive signal transduction cascade in yeast. The specificity of Krs-1 and Krs-2 activation and their similarity to Ste20p suggest that they may function at an early step in phosphorylation events that are specific responses to some forms of chemical stress or extreme heat shock.