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- W2069299204 abstract "We have shown that MLCK and calmodulin (CaM) co-purify with unphosphorylated SMM (up-SMM) from chicken gizzard, suggesting that they are tightly bound. Although the MLCK:SMM molar ratio in SMM preparations was well below stoichiometric (1:73 ± 9), the ratio was ∼ 23-37% of that in gizzard tissue. Fifteen to 30% of MLCK was associated with CaM at ∼1 nM free [Ca2+]. There were two MLCK pools that bound up-SMM with Kd ∼10 μM and 0.2 μM and phosphorylated SMM with a Kd ∼ 20 μM and 0.2 μM. Using motility assays, co-sedimentation assays, and on-coverslip ELISA assays, we provide strong evidence that most of the MLCK is bound directly to SMM through the telokin domain. The bound MLCK can phosphorylate SMM in a Ca2+-dependent manner with a pCa50 ∼ 6 as measured by in vitro motility, similar to in vivo results. After activation of SMM-bound MLCK/CaM with Ca2+ and ATP, both motility (0.5 μm/sec) and phosphorylation (>15%) of SMM reach a maximum after ∼15-30 min, inconsistent with a free diffusion mechanism. Actin movement over the SMM is not required for this phosphorylation process. Experiments are underway to test the idea that SMM heads proximal to the MLCK-SMM become phosphorylated by a tethered diffusion mechanism." @default.
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- W2069299204 date "2010-01-01" @default.
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- W2069299204 title "Determining Mechanism of Phosphorylation of Smooth Muscle Myosin by Calmodulin-Myosin Light Chain Kinase Using an in vitro Model System" @default.
- W2069299204 doi "https://doi.org/10.1016/j.bpj.2009.12.2236" @default.
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