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Activation of the cell integrity pathway is channelled through diverse signalling elements in fission yeast

机译：细胞完整性途径的激活通过裂变酵母中的多种信号传导途径进行引导

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摘要

MAPK Pmk1p is the central element of a cascade involved in the maintenance of cell integrity and other functions in Schizosaccharomyces pombe. Pmk1p becomes activated by multiple stressing situations and also during cell separation. GTPase Rho2p acts upstream of the protein kinase C homolog Pck2p to activate the Pmk1 signalling pathway through direct interaction with MAPKKK Mkh1p. In this work we analyzed the functional significance of both Rho2p and Pck2p in the transduction of various stress signals by the cell integrity pathway. The results indicate that basal Pmk1p activity can be positively regulated by alternative mechanisms which are independent on the control by Rho2p and/or Pck2p. Unexpectedly, Pck1p, another protein kinase C homolog, negatively modulates Pmk1p basal activity by an unknown mechanism. Moreover, different elements appear to regulate the stress-induced activation of Pmk1p depending on the nature of the triggering stimuli. Whereas Pmk1p activation induced by hyper- or hypotonic stresses is channeled through Rho2p-Pck2p, other stressors, like glucose deprivation or cell wall disturbance, are transduced via other pathways in addition to that of Rho2p-Pck2p. On the contrary, Pmk1p activation observed during cell separation or after treatment with hydrogen peroxide does not involve Rho2p-Pck2p. Finally, Pck2p function is critical to maintain a Pmk1p basal activity that allows Pmk1p activation induced by heat stress. These data demonstrate the existence of a complex signalling network modulating Pmk1p activation in response to a variety of stresses in fission yeast. (C) 2008 Elsevier Inc. All rights reserved.
机译：MAPK Pmk1p是级联的中心元素，参与维持粟酒裂殖酵母中的细胞完整性和其他功能。 Pmk1p在多种应激情况下以及细胞分离过程中均被激活。 GTPase Rho2p在蛋白激酶C同源物Pck2p的上游起作用，通过与MAPKKK Mkh1p直接相互作用来激活Pmk1信号传导途径。在这项工作中，我们分析了Rho2p和Pck2p在通过细胞完整性途径转导各种应激信号中的功能意义。结果表明，基础Pmk1p活性可以由替代机制积极调控，而独立于Rho2p和/或Pck2p的控制。出乎意料的是，另一种蛋白激酶C同源物Pck1p通过未知机制负调控Pmk1p基础活性。此外，取决于触发刺激的性质，不同的元素似乎可以调节应激诱导的Pmk1p激活。高渗或低渗应激诱导的Pmk1p激活通过Rho2p-Pck2p传导，而除Rho2p-Pck2p之外，其他应激源（如葡萄糖剥夺或细胞壁紊乱）也通过其他途径转导。相反，在细胞分离过程中或用过氧化氢处理后观察到的Pmk1p激活不涉及Rho2p-Pck2p。最后，Pck2p功能对于维持允许由热应激诱导的Pmk1p激活的Pmk1p基础活性至关重要。这些数据表明存在一个复杂的信号网络，该网络调节裂变酵母中的多种应激，从而调节Pmk1p的激活。 （C）2008 Elsevier Inc.保留所有权利。

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