 Abstract cell migration is essential for cancer spreading. AMP-activated protein kinase, AMPK, regulates cell migration by acting as a molecular hub that senses adhesions and controls mitochondria and cytoskeleton. In three-dimensional matrices, low adhesion leads to low ATP-AMP levels, which activate AMPK and cause mitochondrial fission, decreasing oxidative phosphorylation and reducing ATP production. At the same time, AMPK inhibits myosin phosphatase, promoting myosin 2, mediated amoeboid migration. This mechanism is reversed when AMPK is inhibited, thus suppressing metastasis of amoeboid cancer cells in vivo. Furthermore, this study shows that AMPK is also involved in regulating mitochondrial dynamics and cytoskeleton, suggesting that it is a metanometabolic sensor that links energy production with cell motility. This article was authored by Eva Crozes-Mollist, Vittoria Graziani, Oscar Makes, and others. We are article.tv, links in the description below.