Members of the Arabidopsis calcineurin B-like Ca2+ binding protein (AtCBL)
family are differentially regulated by stress conditions. One AtCBL plays a
role in salt stress; another is implicated in response to other stress sig
nals, including drought, cold, and wounding. In this study, we identified a
group of novel protein kinases specifically associated with AtCBL-type Ca2
+ sensors. In addition to a typical protein kinase domain, they all contain
a unique C-terminal region that is both required and sufficient for intera
ction with the AtCBL-type but not calmodulin-type Ca2+ binding proteins fro
m plants. Interactions between the kinases and AtCBLs require micromolar co
ncentrations of Ca2+, suggesting that increases in cellular Ca2+ concentrat
ions may trigger the formation of AtCBL-kinase complexes in vivo. Unlike mo
st serine/threonine kinases, the AtCBL-interacting kinase efficiently uses
Mn2+ to Mg2+ as a cofactor and may function as a Mn2+ binding protein in th
e cell. These findings link a new type of Ca2+ sensors to a group of novel
protein kinases, providing the molecular basis for a unique Ca2+ signaling
machinery in plant cells.