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首页> 外文期刊>Cell metabolism >KSR2 is an essential regulator of AMP kinase, energy expenditure, and insulin sensitivity.
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KSR2 is an essential regulator of AMP kinase, energy expenditure, and insulin sensitivity.

机译：KSR2是AMP激酶，能量消耗和胰岛素敏感性的重要调节剂。

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Kinase suppressors of Ras 1 and 2 (KSR1 and KSR2) function as molecular scaffolds to potently regulate the MAP kinases ERK1/2 and affect multiple cell fates. Here we show that KSR2 interacts with and modulates the activity of AMPK. KSR2 regulates AMPK-dependent glucose uptake and fatty acid oxidation in mouse embryonic fibroblasts and glycolysis in a neuronal cell line. Disruption of KSR2 in vivo impairs AMPK-regulated processes affecting fatty acid oxidation and thermogenesis to cause obesity. Despite their increased adiposity, ksr2(-/-) mice are hypophagic and hyperactive but expend less energy than wild-type mice. In addition, hyperinsulinemic-euglycemic clamp studies reveal that ksr2(-/-) mice are profoundly insulin resistant. The expression of genes mediating oxidative phosphorylation is also downregulated in the adipose tissue of ksr2(-/-) mice. These data demonstrate that ksr2(-/-) mice are highly efficient in conserving energy, revealing a novel role for KSR2 in AMPK-mediated regulation of energy metabolism.
机译：Ras 1和2（KSR1和KSR2）的激酶抑制剂作为分子支架，可有效调节MAP激酶ERK1 / 2并影响多种细胞命运。在这里，我们显示KSR2与AMPK相互作用并调节其活性。 KSR2调节小鼠胚胎成纤维细胞中AMPK依赖的葡萄糖摄取和脂肪酸氧化以及神经元细胞系中的糖酵解。体内KSR2的破坏会破坏AMPK调控的过程，影响脂肪酸氧化和生热，从而导致肥胖。尽管它们的肥胖增加，但ksr2（-/-）小鼠的吞噬能力和活动过度，但消耗的能量少于野生型小鼠。此外，高胰岛素-正常血糖钳夹研究显示ksr2（-/-）小鼠对胰岛素具有很高的抵抗力。 ksr2（-/-）小鼠的脂肪组织中介导氧化磷酸化的基因的表达也下调。这些数据表明ksr2（-/-）小鼠在节能方面非常高效，揭示了KSR2在AMPK介导的能量代谢调节中的新作用。

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