Calcium Calmodulin Kinase Kinase 2
CaMKK2 was originally purified and characterized from rat brain as a CaMKI-activating kinase by Edelman et al. (1996). These authors demonstrated that CaMKK2 activated CaMKI and CaMKIV by phosphorylating an equivalent Thr residue within the “activation loop” region of both proteins. Later, rat and human CaMKK2 were cloned and characterized by two independent groups, which provided substantial information about the structure and function of CaMKK2 (Anderson et al. 1998; Kitani et al. 1997). The cAMP-activated protein kinase (AMPK) was subsequently identified as an additional substrate of CaMKK2 in 2005 (Hawley et al. 2005; Woods et al. 2005). The discovery of AMPK as a downstream target of CaMKK2 was an important milestone, which opened new research perspectives, providing mechanistic evidence for...
Pilot grant from the Opportunity Funds Management Core of the Centers for Medical Countermeasures against Radiation, National Institute of Allergy and Infectious Diseases; grant number U19AI067773 awarded to L.R
- Edelman AM, et al. Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence. J Biol Chem. 1996;271:10806–10.Google Scholar
- Luo XJ, et al. Convergent lines of evidence support CAMKK2 as a schizophrenia susceptibility gene. Mol Psychiatry. 2014;19:774–83.Google Scholar
- Scott JW, et al. Autophosphorylation of CaMKK2 generates autonomous activity that is disrupted by a T85S mutation linked to anxiety and bipolar disorder. Sci Rep. 2015;5:14436.Google Scholar