Tzatsos Alexandros, Tsichlis Philip N
Molecular Oncology Research Institute, Tufts-New England Medical Center, Boston, Massachusetts 02111.
Molecular Oncology Research Institute, Tufts-New England Medical Center, Boston, Massachusetts 02111.
J Biol Chem. 2007 Jun 22;282(25):18069-18082. doi: 10.1074/jbc.M610101200. Epub 2007 Apr 25.
Energy depletion activates AMP-activated protein kinase (AMPK) and inhibits cell growth via TSC2-dependent suppression of mTORC1 signaling. Long term energy depletion also induces apoptosis by mechanisms that are not well understood to date. Here we show that AMPK, activated by energy depletion, inhibited cell survival by binding to and phosphorylating IRS-1 at Ser-794. Phosphorylation of IRS-1 at this site inhibited phosphatidylinositol 3-kinase/Akt signaling, suppressed the mitochondrial membrane potential, and promoted apoptosis. Of the treatments promoting energy depletion, glucose deprivation, hypoxia, and inhibition of ATP synthesis in the mitochondria stimulated phosphorylation of IRS-1 at Ser-794 via an LKB1/AMPK-dependent manner, whereas oxidative stress and 2-deoxyglucose stimulated phosphorylation at this site via a Ca2+/calmodulin-dependent protein kinase kinase beta/AMPK axis. These data define a novel pathway that cooperates with other adaptive mechanisms to formulate the cellular response to energy depletion.
能量耗竭激活AMP活化蛋白激酶(AMPK),并通过TSC2依赖的mTORC1信号抑制作用来抑制细胞生长。长期能量耗竭还通过迄今尚未完全了解的机制诱导细胞凋亡。在此,我们表明,由能量耗竭激活的AMPK通过与IRS-1结合并使其在Ser-794位点磷酸化,从而抑制细胞存活。IRS-1在此位点的磷酸化抑制磷脂酰肌醇3激酶/Akt信号传导,抑制线粒体膜电位,并促进细胞凋亡。在促进能量耗竭的处理中,葡萄糖剥夺、缺氧和线粒体中ATP合成的抑制通过LKB1/AMPK依赖性方式刺激IRS-1在Ser-794位点的磷酸化,而氧化应激和2-脱氧葡萄糖则通过Ca2+/钙调蛋白依赖性蛋白激酶激酶β/AMPK轴刺激该位点的磷酸化。这些数据定义了一条新的途径,该途径与其他适应性机制协同作用,以形成细胞对能量耗竭的反应。