T. A. Hornberger: Department of Comparative Biosciences, 2015 Linden Drive, Madison, WI 53706, USA.
J Physiol. 2013 Sep 15;591(18):4611-20. doi: 10.1113/jphysiol.2013.256339. Epub 2013 Jun 3.
The goal of this study was to determine whether the mechanical activation of mechanistic target of rapamycin (mTOR) signalling is associated with changes in phosphorylation of tuberous sclerosis complex-2 (TSC2) and targeting of mTOR and TSC2 to the lysosome. As a source of mechanical stimulation, mouse skeletal muscles were subjected to eccentric contractions (ECs). The results demonstrated that ECs induced hyper-phosphorylation of TSC2 and at least part of this increase occurred on residue(s) that fall within RxRxxS/T consensus motif(s). Furthermore, in control muscles, we found that both mTOR and TSC2 are highly enriched at the lysosome. Intriguingly, ECs enhanced the lysosomal association of mTOR and almost completely abolished the lysosomal association of TSC2. Based on these results, we developed a new model that could potentially explain how mechanical stimuli activate mTOR signalling. Furthermore, this is the first study to reveal that the activation of mTOR is associated with the translocation of TSC2 away from the lysosome. Since a large number of signalling pathways rely on TSC2 to control mTOR signalling, our results have potentially revealed a fundamental mechanism via which not only mechanical, but also various other types of stimuli, control mTOR signalling.
本研究旨在确定机械激活雷帕霉素靶蛋白(mTOR)信号是否与结节性硬化复合物 2(TSC2)的磷酸化变化以及 mTOR 和 TSC2 向溶酶体的靶向有关。作为机械刺激的来源,我们使小鼠骨骼肌经历离心收缩(ECs)。结果表明,ECs 诱导 TSC2 的过度磷酸化,并且至少部分增加发生在位于 RxRxxS/T 共有基序内的残基上。此外,在对照肌肉中,我们发现 mTOR 和 TSC2 都高度富集在溶酶体上。有趣的是,ECs 增强了 mTOR 与溶酶体的结合,并几乎完全消除了 TSC2 与溶酶体的结合。基于这些结果,我们提出了一个新的模型,该模型可能解释了机械刺激如何激活 mTOR 信号。此外,这是第一项揭示 mTOR 激活与 TSC2 从溶酶体易位相关的研究。由于大量信号通路依赖于 TSC2 来控制 mTOR 信号,我们的结果可能揭示了一种基本机制,通过这种机制,不仅是机械刺激,而且还有各种其他类型的刺激,都可以控制 mTOR 信号。