Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Biochem Biophys Res Commun. 2012 Apr 27;421(1):1-3. doi: 10.1016/j.bbrc.2012.04.010. Epub 2012 Apr 7.
AMP-activated protein kinase (AMPK) is an essential enzyme indispensable for energy sensing and metabolic homeostasis at both the cellular and whole-body levels. Phosphorylation of AMPK, a key step for its activation, is known to be regulated by upstream kinases such as liver kinase B1 (LKB1) and calmodulin-dependent protein kinase kinase-beta (CaMKKβ). Recent evidence shows that inositol polyphosphate multikinase (IPMK), which possesses both inositol phosphate kinase and lipid inositol kinase activities, can physiologically regulate AMPK signaling in cultured cells and in the arcuate nucleus. IPMK-mediated regulation of AMPK occurs through the dynamic protein interactions of IPMK with AMPK in response to glucose availability. Here we review and discuss a novel role for the hypothalamic IPMK signaling in the control of AMPK and central energy homeostasis.
腺苷酸活化蛋白激酶(AMPK)是一种必需的酶,在细胞和全身水平上对能量感应和代谢稳态至关重要。AMPK 的磷酸化是其激活的关键步骤,已知受上游激酶如肝激酶 B1(LKB1)和钙调蛋白依赖性蛋白激酶激酶-β(CaMKKβ)的调节。最近的证据表明,肌醇多磷酸激酶(IPMK)具有肌醇磷酸激酶和脂质肌醇激酶活性,可在培养细胞和弓状核中生理调节 AMPK 信号。IPMK 通过响应葡萄糖可用性与 AMPK 的动态蛋白相互作用来调节 AMPK。在这里,我们回顾和讨论了下丘脑 IPMK 信号在 AMPK 和中枢能量稳态控制中的新作用。