Dissecting cooperative calmodulin binding to CaM kinase II: a detailed stochastic model

被引:22
作者
Byrne, Michael J. [1 ]
Putkey, John A. [2 ]
Waxham, M. Neal [1 ]
Kubota, Yoshihisa [1 ]
机构
[1] Univ Texas Houston, Dept Neurobiol & Anat, Sch Med, Houston, TX 77030 USA
[2] Univ Texas Houston, Dept Biochem & Mol Biol, Sch Med, Houston, TX 77030 USA
关键词
Calmodulin; CaMKII; Synaptic plasticity; Gillespie algorithm; Particle swarm theory; 2-PHOTON CROSS-CORRELATION; PROTEIN-KINASE; CALCIUM-BINDING; TERMINAL DOMAIN; CA2+ CHANNEL; TROPONIN-I; MECHANISMS; COMPLEX; STOICHIOMETRY; DISSOCIATION;
D O I
10.1007/s10827-009-0173-3
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:621 / 638
页数:18
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