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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2001-1-11
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pubmed:abstractText |
A mathematical model is presented of autophosphorylation of Ca(2+)/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 Ca(2+) concentration range from below the resting value of the intracellular [Ca(2+)] 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. Ca(2+) 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 Ca(2+) 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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2211-21
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
pubmed-meshheading:11053103-Animals,
pubmed-meshheading:11053103-Biophysical Phenomena,
pubmed-meshheading:11053103-Biophysics,
pubmed-meshheading:11053103-Brain,
pubmed-meshheading:11053103-Calcium Signaling,
pubmed-meshheading:11053103-Calcium-Calmodulin-Dependent Protein Kinase Type 2,
pubmed-meshheading:11053103-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:11053103-Enzyme Stability,
pubmed-meshheading:11053103-Kinetics,
pubmed-meshheading:11053103-Long-Term Potentiation,
pubmed-meshheading:11053103-Models, Biological,
pubmed-meshheading:11053103-Mutagenesis, Site-Directed,
pubmed-meshheading:11053103-Phosphoprotein Phosphatases,
pubmed-meshheading:11053103-Phosphorylation,
pubmed-meshheading:11053103-Synapses
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pubmed:year |
2000
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pubmed:articleTitle |
Bistability in the Ca(2+)/calmodulin-dependent protein kinase-phosphatase system.
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pubmed:affiliation |
Department of Chemistry and Volen Center for Complex Systems, Brandeis University, Waltham, Massachusetts 02454-9110, USA. zhabotinsky@brandeis.edu
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