Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells.

By A. Woods, Kristina Dickerson, R. Heath, Seung-pyo Hong, M. Momcilovic, S. Johnstone, M. Carlson, David Carling. Cell Metabolism, 2005

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AMPK and TOR: The Yin and Yang of Cellular Nutrient Sensing and Growth Control. (2020, background): “…and by DNA damage 212 Thr172 can also be phosphorylated by alternate upstream kinases, including the Ca2+/calmodulin-213 dependent kinase, CaMKK2 (Hawley et al., 2005; Hurley et al., 2005; Woods et al., 2005) and 214 TAK1 (Transforming growth factor-b-Activated Kinase-1) (Momcilovic et al., 2006).”
An AMPK-FOXO pathway mediates longevity induced by a novel method of dietary restriction in C. elegans. (2007, neutral): “AMP binding to the γ subunit induces a conformational change that allows the catalytic α subunit to be phosphorylated and activated by the AMPK-activating protein kinases LKB1 and CAMKKβ [9–13].”
AMP‐activated protein kinase – development of the energy sensor concept (2006, background): “In a rapid flurry of activity, evidence was obtained that all three, but especially LKB1 and CaMKKβ, can phosphorylate Thr-172 and thus activate AMPK in intact cells and in vivo (Hawley et al. 2003, 2005; Woods et al. 2003, 2005; Shaw et al. 2004; Hurley et al. 2005; Sakamoto et al. 2005, 2006).”