Name
Title | ||
|---|---|---|
Dissecting cooperative calmodulin binding to CaM kinase II: a detailed stochastic model. |
Abstract | ||
|---|---|---|
Calmodulin (CaM) is a major Ca2+ binding protein involved in two opposing processes of synaptic plasticity of CA1 pyramidal neurons: long-term potentiation
(LTP) and depression (LTD). The N- and C-terminal lobes of CaM bind to its target separately but cooperatively and introduce
complex dynamics that cannot be well understood by experimental measurement. Using a detailed stochastic model constructed
upon experimental data, we have studied the interaction between CaM and Ca2+-CaM-dependent protein kinase II (CaMKII), a key enzyme underlying LTP. The model suggests that the accelerated binding of
one lobe of CaM to CaMKII, when the opposing lobe is already bound to CaMKII, is a critical determinant of the cooperative
interaction between Ca2+, CaM, and CaMKII. The model indicates that the target-bound Ca2+ free N-lobe has an extended lifetime and may regulate the Ca2+ response of CaMKII during LTP induction. The model also reveals multiple kinetic pathways which have not been previously
predicted for CaM-dissociation from CaMKII. |
Year | DOI | Venue |
|---|---|---|
2009 | 10.1007/s10827-009-0173-3 | Journal of Computational Neuroscience |
Keywords | Field | DocType |
Calmodulin,CaMKII,Synaptic plasticity,Gillespie algorithm,Particle swarm theory | Long-term potentiation,Neuroscience,Binding site,Control theory,Biophysics,Binding protein,Calmodulin,Ca2+/calmodulin-dependent protein kinase,Synaptic plasticity,Calcium signaling,LTP induction,Mathematics | Journal |
Volume | Issue | ISSN |
27 | 3 | 1573-6873 |
Citations | PageRank | References |
4 | 0.81 | 0 |
Authors | ||
4 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| Michael J. Byrne | 1 | 23 | 3.73 |
| John A. Putkey | 2 | 4 | 1.14 |
| M Neal Waxham | 3 | 23 | 3.83 |
| Y Kubota | 4 | 36 | 8.75 |