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首页> 外文期刊>Molecular and Cellular Biology >Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7.
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Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7.

机译：酵母信息素反应途径中的信号：丝裂原活化蛋白（MAP）激酶Kss1和Fus3与上游MAP激酶激酶Ste7的特异性和高亲和力相互作用。

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Kss1 and Fus3 are mitogen-activated protein kinases (MAPKs or ERKs), and Ste7 is their activating MAPK/ERK kinase (MEK), in the pheromone response pathway of Saccharomyces cerevisiae. To investigate the potential role of specific interactions between these enzymes during signaling, their ability to associate with each other was examined both in solution and in vivo. When synthesized by in vitro translation, Kss1 and Fus3 could each form a tight complex (Kd of approximately 5 nM) with Ste7 in the absence of any additional yeast proteins. These complexes were specific because neither Hog1 nor Mpk1 (two other yeast MAPKs), nor mammalian Erk2, was able to associate detectably with Ste7. Neither the kinase catalytic core of Ste7 nor the phosphoacceptor regions of Ste7 and Kss1 were necessary for complex formation. Ste7-Kss1 (and Ste7-Fus3) complexes were present in yeast cell extracts and were undiminished in extracts prepared from a ste5delta-ste11delta double mutant strain. In Ste7-Kss1 (or Ste7-Fus3) complexes isolated from naive or pheromone-treated cells, Ste7 phosphorylated Kss1 (or Fus3), and Kss1 (or Fus3) phosphorylated Ste7, in a pheromone-stimulated manner; dissociation of the high-affinity complex was shown to be required for either phosphorylation event. Deletions of Ste7 in the region required for its stable association with Kss1 and Fus3 in vitro significantly decreased (but did not eliminate) signaling in vivo. These findings suggest that the high-affinity and active site-independent binding observed in vitro facilitates signal transduction in vivo and suggest further that MEK-MAPK interactions may utilize a double-selection mechanism to ensure fidelity in signal transmission and to insulate one signaling pathway from another.
机译：在酿酒酵母的信息素反应途径中，Kss1和Fus3是促分裂原激活的蛋白激酶（MAPKs或ERKs），Ste7是其激活的MAPK / ERK激酶（MEK）。为了研究这些酶在信号传导过程中特异性相互作用的潜在作用，在溶液和体内均检查了它们彼此缔合的能力。当通过体外翻译合成时，Kss1和Fus3可以在没有任何其他酵母蛋白的情况下与Ste7形成紧密的复合物（Kd约为5 nM）。这些复合物具有特异性，因为Hog1和Mpk1（另外两种酵母MAPKs）或哺乳动物Erk2都无法与Ste7进行检测。 Ste7的激酶催化核心以及Ste7和Kss1的磷酸受体区域都不是形成复合物所必需的。 Ste7-Kss1（和Ste7-Fus3）复合物存在于酵母细胞提取物中，并且在由ste5delta-ste11delta双突变株制备的提取物中没有减弱。从幼稚或信息素处理的细胞中分离出的Ste7-Kss1（或Ste7-Fus3）复合物中，以信息素刺激的方式将Ste7磷酸化Kss1（或Fus3）和Kss1（或Fus3）磷酸化Ste7。高亲和力复合物的解离被证明是任一磷酸化事件所必需的。在体内与Kss1和Fus3稳定缔合所需的区域中，Ste7的缺失显着减少（但并未消除）体内的信号传导。这些发现表明，在体外观察到的高亲和力和活性位点无关的结合促进了体内信号转导，并进一步表明，MEK-MAPK相互作用可能利用双重选择机制来确保信号传递的保真度并从中隔离一条信号通路。另一个。

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