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Biophys J, November 2000, p. 2211-2221, Vol. 79, No. 5

Bistability in the Ca2+/Calmodulin-Dependent Protein Kinase-Phosphatase System

Anatol M. Zhabotinsky

Department of Chemistry and Volen Center for Complex Systems, Brandeis University, Waltham, Massachusetts 02454-9110 USA

A mathematical model is presented of autophosphorylation of Ca2+/calmodulin-dependent protein kinase (CaMKII) and its dephosphorylation by a phosphatase. If the total concentration of CaMKII subunits is significantly higher than the phosphatase Michaelis constant, two stable steady states of the CaMKII autophosphorylation can exist in a Ca2+ concentration range from below the resting value of the intracellular [Ca2+] to the threshold concentration for induction of long-term potentiation (LTP). Bistability is a robust phenomenon, it occurs over a wide range of parameters of the model. Ca2+ transients that switch CaMKII from the low-phosphorylated state to the high-phosphorylated one are in the same range of amplitudes and frequencies as the Ca2+ transients that induce LTP. These results show that the CaMKII-phosphatase bistability may play an important role in long-term synaptic modifications. They also suggest a plausible explanation for the very high concentrations of CaMKII found in postsynaptic densities of cerebral neurons.

Biophys J, November 2000, p. 2211-2221, Vol. 79, No. 5
© 2000 by the Biophysical Society   0006-3495/00/11/2211/11  $2.00


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