Systems Biology Ireland, University College Dublin Dublin, Ireland.
Front Physiol. 2012 Sep 18;3:355. doi: 10.3389/fphys.2012.00355. eCollection 2012.
Mitogen-activated protein kinase (MAPK) cascades control cell fate decisions, such as proliferation, differentiation, and apoptosis by integrating and processing intra- and extracellular cues. However, similar MAPK kinetic profiles can be associated with opposing cellular decisions depending on cell type, signal strength, and dynamics. This implies that signaling by each individual MAPK cascade has to be considered in the context of the entire MAPK network. Here, we develop a dynamic model of feedback and crosstalk for the three major MAPK cascades; extracellular signal-regulated kinase (ERK), p38 mitogen-activated protein kinase (p38), c-Jun N-terminal kinase (JNK), and also include input from protein kinase B (AKT) signaling. Focusing on the bistable activation characteristics of the JNK pathway, this model explains how pathway crosstalk harmonizes different MAPK responses resulting in pivotal cell fate decisions. We show that JNK can switch from a transient to sustained activity due to multiple positive feedback loops. Once activated, positive feedback locks JNK in a highly active state and promotes cell death. The switch is modulated by the ERK, p38, and AKT pathways. ERK activation enhances the dual specificity phosphatase (DUSP) mediated dephosphorylation of JNK and shifts the threshold of the apoptotic switch to higher inputs. Activation of p38 restores the threshold by inhibiting ERK activity via the PP1 or PP2A phosphatases. Finally, AKT activation inhibits the JNK positive feedback, thus abrogating the apoptotic switch and allowing only proliferative signaling. Our model facilitates understanding of how cancerous deregulations disturb MAPK signal processing and provides explanations for certain drug resistances. We highlight a critical role of DUSP1 and DUSP2 expression patterns in facilitating the switching of JNK activity and show how oncogene induced ERK hyperactivity prevents the normal apoptotic switch explaining the failure of certain drugs to induce apoptosis.
丝裂原活化蛋白激酶(MAPK)级联反应通过整合和处理细胞内外信号来控制细胞命运决定,如增殖、分化和凋亡。然而,类似的 MAPK 动力学特征可能与细胞类型、信号强度和动力学有关,导致相反的细胞决策。这意味着,应该在整个 MAPK 网络的背景下考虑每个单独的 MAPK 级联的信号传递。在这里,我们为三种主要的 MAPK 级联(细胞外信号调节激酶(ERK)、p38 丝裂原活化蛋白激酶(p38)、c-Jun N 端激酶(JNK))开发了一个反馈和串扰的动态模型,同时也包括蛋白激酶 B(AKT)信号的输入。我们专注于 JNK 途径的双稳态激活特性,该模型解释了途径串扰如何协调不同的 MAPK 反应,从而导致关键的细胞命运决定。我们表明,JNK 可以由于多个正反馈回路而从短暂活性转变为持续活性。一旦被激活,正反馈就会将 JNK 锁定在高度活跃的状态,并促进细胞死亡。这种转变受 ERK、p38 和 AKT 途径的调节。ERK 的激活通过双重特异性磷酸酶(DUSP)介导的 JNK 去磷酸化增强,从而将凋亡开关的阈值提高到更高的输入。p38 的激活通过 PP1 或 PP2A 磷酸酶抑制 ERK 活性来恢复阈值。最后,AKT 的激活抑制 JNK 的正反馈,从而消除凋亡开关并仅允许增殖信号。我们的模型有助于理解致癌失调如何干扰 MAPK 信号处理,并为某些药物抗性提供解释。我们强调 DUSP1 和 DUSP2 表达模式在促进 JNK 活性转换中的关键作用,并展示了致癌基因诱导的 ERK 过度活跃如何防止正常的凋亡开关,解释了某些药物诱导凋亡失败的原因。