Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase.

By S. Hawley, D. A. Pan, K. J. Mustard, Louise Ross, J. Bain, A. Edelman, B. Frenguelli, D. Hardie. Cell Metabolism, 2005

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Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation (2010, background): “, 2006) and phenformin (Hawley et al., 2005) have been reported to alter adenine nucleotide ratios in cultured cells, activation by metformin was seen under conditions where no such changes were detectable (Fryer et al.”
Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases (2012, positive): “Activation of AMPK via energy depletion is thought to be dependent on LKB1, and activation of AMPK via increased intracellular Ca2+ is dependent on CamKKβ (Hawley et al., 2005; Hurley et al., 2005; Woods et al., 2005).”
The AMP-activated protein kinase (AMPK) signaling pathway coordinates cell growth, autophagy, & metabolism (2011, positive): “Importantly, AMPK can also be phosphorylated on Thr 172 in response to calcium flux, independently of LKB1, through CAMKK2 (also known as CAMKKβ) kinase, which is the closest mammalian kinase to LKB1 by sequence homolog”
Resistance exercise increases AMPK activity and reduces 4E‐BP1 phosphorylation and protein synthesis in human skeletal muscle (2006, background): “Although recent work suggests that calmodulin-dependent protein kinase kinaseβ can phosphorylate and activate AMPK (Hawley et al. 2005; Woods et al. 2005), its role in skeletal muscle is probably minor because the expression of this kinase in muscle is extremely low.”