Cooperative Dependence of the Actin-activated Mg2+-ATPase Activity of Acanthamoeba Myosin II on the Extent of Filament Phosphorylation
Population
Acanthamoeba castellanii myosin II
Comparison
Chemical modification with N-ethylmaleimide and… vs Native phosphorylated myosin II alone, or…
Design
Preclinical
Authors
Discussion
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Member takes
Implication
May inform models of myosin filament regulation; leaves open relevance to cardiac contractility in vivo.
Structured PICO
P
Population
Acanthamoeba castellanii myosin II
I
Intervention
Chemical modification with N-ethylmaleimide (NEM) and co-polymerization of phosphorylated and dephosphorylated myosin II
C
Comparator
Native phosphorylated myosin II alone, or dephosphorylated myosin II alone
O
Outcome
Actin-activated Mg2+-ATPase activitysurrogate
The specific activity of each myosin II molecule within a filament is highly cooperatively dependent upon the state of phosphorylation of the filament as a whole, rather than its own phosphorylation state.
Cite This Study
Atkinson et al. (1989) studied this question.