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Multifunctional calcium/calmodulin-dependent protein kinase



Multifunctional calcium/calmodulin-dependent protein kinase



Neurochemical Research 18(1): 65-77



Multifunctional Ca-2+/calmodulin-dependent protein kinase (CaM kinase) is a prominent mediator of neutroransmitters which elevate Ca-2+. It coordinates cellular responses to external stimuli by phosphorylating proteins involved in neurotransmitter synthesis, neurotransmitter release, carbohydrate metabolism, ion flux and neuronal plasticity. Structure/function studies of CaM kinase have provided insights into how it decodes Ca-2+ signals. The kinase is kept relatively inactive in its basal state by the presence of an autoinhibitory domain. Binding of Ca-2+/calmodulin eliminates this inhibitory constraint and allows the kinase to phosphorylate its substrates, as well as itself. This autophosphorylation significantly slows dissociation of calmodulin, thereby trapping calmodulin even when Ca-2+ levels are subthreshold. The kinase may respond particularly well to multiple Ca-2+ spikes since trapping may enable a spike frequency-dependent recruitment of calmodulin with each successive Ca-2+ spike leading to increased activation of the kinase. Once calmodulin dissociates, CaM kinase remains partially active until it is dephosphorylated, providing for an additional period in which its response to brief Ca-2+ trnasients is potentiated.

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