Nim Tri Hieu, Luo Le, White Jacob K, Clément Marie-Véronique, Tucker-Kellogg Lisa
Computational Systems Biology Programme, Singapore-MIT Alliance, Singapore.
Systems Biology Institute (SBI), Clayton, Victoria, Australia.
PLoS Comput Biol. 2015 Nov 10;11(11):e1004505. doi: 10.1371/journal.pcbi.1004505. eCollection 2015 Nov.
The dynamic behaviors of signaling pathways can provide clues to pathway mechanisms. In cancer cells, excessive phosphorylation and activation of the Akt pathway is responsible for cell survival advantages. In normal cells, serum stimulation causes brief peaks of extremely high Akt phosphorylation before reaching a moderate steady-state. Previous modeling assumed this peak and decline behavior (i.e., "overshoot") was due to receptor internalization. In this work, we modeled the dynamics of the overshoot as a tool for gaining insight into Akt pathway function. We built an ordinary differential equation (ODE) model describing pathway activation immediately upstream of Akt phosphorylation at Thr308 (Aktp308). The model was fit to experimental measurements of Aktp308, total Akt, and phosphatidylinositol (3,4,5)-trisphosphate (PIP3), from mouse embryonic fibroblasts with serum stimulation. The canonical Akt activation model (the null hypothesis) was unable to recapitulate the observed delay between the peak of PIP3 (at 2 minutes), and the peak of Aktp308 (at 30-60 minutes). From this we conclude that the peak and decline behavior of Aktp308 is not caused by PIP3 dynamics. Models for alternative hypotheses were constructed by allowing an arbitrary dynamic curve to perturb each of 5 steps of the pathway. All 5 of the alternative models could reproduce the observed delay. To distinguish among the alternatives, simulations suggested which species and timepoints would show strong differences. Time-series experiments with membrane fractionation and PI3K inhibition were performed, and incompatible hypotheses were excluded. We conclude that the peak and decline behavior of Aktp308 is caused by a non-canonical effect that retains Akt at the membrane, and not by receptor internalization. Furthermore, we provide a novel spline-based method for simulating the network implications of an unknown effect, and we demonstrate a process of hypothesis management for guiding efficient experiments.
信号通路的动态行为可为通路机制提供线索。在癌细胞中,Akt通路的过度磷酸化和激活赋予细胞生存优势。在正常细胞中,血清刺激会导致Akt磷酸化出现短暂的极高峰值,随后达到中等稳态。先前的模型认为这种峰值和下降行为(即“过冲”)是由于受体内化所致。在本研究中,我们将过冲的动力学建模作为深入了解Akt通路功能的工具。我们构建了一个常微分方程(ODE)模型,描述在苏氨酸308(Aktp308)处Akt磷酸化上游紧邻区域的通路激活情况。该模型与来自经血清刺激的小鼠胚胎成纤维细胞的Aktp308、总Akt和磷脂酰肌醇(3,4,5)-三磷酸(PIP3)的实验测量值进行拟合。经典的Akt激活模型(零假设)无法重现观察到的PIP3峰值(在2分钟时)与Aktp308峰值(在30 - 60分钟时)之间的延迟。由此我们得出结论,Aktp308的峰值和下降行为并非由PIP3动力学引起。通过允许任意动态曲线干扰通路的5个步骤中的每一步,构建了替代假设的模型。所有5个替代模型都能重现观察到的延迟。为了区分这些替代模型,模拟结果表明哪些物种和时间点会显示出强烈差异。进行了膜分级分离和PI3K抑制的时间序列实验,并排除了不相容的假设。我们得出结论,Aktp308的峰值和下降行为是由一种非经典效应引起的,这种效应使Akt保留在膜上,而非受体内化所致。此外,我们提供了一种基于样条的新颖方法来模拟未知效应的网络影响,并展示了一个用于指导高效实验的假设管理过程。