Chruscinski Andrzej J, Singh Harvir, Chan Steven M, Utz Paul J
Division of Cardiology and Heart Transplantation, Department of Medicine, Toronto General Hospital, Toronto, Ontario, Canada.
PLoS One. 2013 Dec 5;8(12):e82164. doi: 10.1371/journal.pone.0082164. eCollection 2013.
β-adrenergic receptors (β-ARs) are model G-protein coupled receptors that mediate signal transduction in the sympathetic nervous system. Despite the widespread clinical use of agents that target β-ARs, the signaling pathways that operate downstream of β-AR stimulation have not yet been completely elucidated. Here, we utilized a lysate microarray approach to obtain a broad-scale perspective of phosphoprotein signaling downstream of β-AR. We monitored the time course of phosphorylation states of 54 proteins after β-AR activation mouse embryonic fibroblast (MEF) cells. In response to stimulation with the non-selective β-AR agonist isoproterenol, we observed previously described phosphorylation events such as ERK1/2(T202/Y204) and CREB(S133), but also novel phosphorylation events such as Cdc2(Y15) and Pyk2(Y402). All of these events were mediated through cAMP and PKA as they were reproduced by stimulation with the adenylyl cyclase activator forskolin and were blocked by treatment with H89, a PKA inhibitor. In addition, we also observed a number of novel isoproterenol-induced protein dephosphorylation events in target substrates of the PI3K/AKT pathway: GSK3β(S9), 4E-BP1(S65), and p70s6k(T389). These dephosphorylations were dependent on cAMP, but were independent of PKA and correlated with reduced PI3K/AKT activity. Isoproterenol stimulation also led to a cAMP-dependent dephosphorylation of PP1α(T320), a modification known to correlate with enhanced activity of this phosphatase. Dephosphorylation of PP1α coincided with the secondary decline in phosphorylation of some PKA-phosphorylated substrates, suggesting that PP1α may act in a feedback loop to return these phosphorylations to baseline. In summary, lysate microarrays are a powerful tool to profile phosphoprotein signaling and have provided a broad-scale perspective of how β-AR signaling can regulate key pathways involved in cell growth and metabolism.
β-肾上腺素能受体(β-ARs)是典型的G蛋白偶联受体,介导交感神经系统中的信号转导。尽管靶向β-ARs的药物在临床上广泛使用,但β-AR刺激下游的信号通路尚未完全阐明。在此,我们利用裂解物微阵列方法获得β-AR下游磷酸化蛋白信号的广泛视角。我们监测了β-AR激活小鼠胚胎成纤维细胞(MEF)后54种蛋白质的磷酸化状态随时间的变化过程。在用非选择性β-AR激动剂异丙肾上腺素刺激后,我们观察到先前描述的磷酸化事件,如ERK1/2(T202/Y204)和CREB(S133),但也观察到新的磷酸化事件,如Cdc2(Y15)和Pyk2(Y402)。所有这些事件均通过cAMP和PKA介导,因为它们可由腺苷酸环化酶激活剂福斯可林刺激重现,并被PKA抑制剂H89处理所阻断。此外,我们还在PI3K/AKT途径的靶底物中观察到一些新的异丙肾上腺素诱导的蛋白质去磷酸化事件:GSK3β(S9)、4E-BP1(S65)和p70s6k(T389)。这些去磷酸化依赖于cAMP,但不依赖于PKA,并且与PI3K/AKT活性降低相关。异丙肾上腺素刺激还导致PP1α(T320)的cAMP依赖性去磷酸化,这种修饰已知与该磷酸酶活性增强相关。PP1α的去磷酸化与一些PKA磷酸化底物磷酸化的二次下降同时发生,表明PP1α可能在反馈回路中起作用,使这些磷酸化恢复到基线水平。总之,裂解物微阵列是分析磷酸化蛋白信号的有力工具,并提供了β-AR信号如何调节细胞生长和代谢中关键途径的广泛视角。