Target intelligence / Profile preview

Actomyosin ATPase

Molecular classification
Enzyme (ATPase, actin-activated), Motor protein complex (actin–myosin complex)
01

Overview

Actomyosin ATPase is the enzyme activity that arises from the interaction of myosin (most often myosin II in muscle) with actin filaments, resulting in ATP hydrolysis coupled to force generation and movement[1][3][4]. In the muscle contractile cycle, binding of ATP to the myosin head causes dissociation from actin, hydrolysis of ATP induces a conformational change in myosin (cocking), and subsequent binding to actin and release of phosphate and ADP drives the power stroke and filament sliding[1][3]. This cycle underlies muscle contraction and many other force-generating processes in cells. Pathological alterations to actomyosin ATPase activity contribute to various muscle and cardiac diseases, and this target is pharmacologically modulated by several drugs for conditions like heart failure and hypertrophic cardiomyopathy[1][3][4].

Other names
Actin-myosin ATPaseMuscle ATPaseMyosin ATPase (when referring to actin-activated ATPase activity)
02

Mechanism of action

Inhibition of ATP hydrolysis (decreases contractility) Activation or sensitization of ATPase (increases contractility)

03

Biological functions

Muscle contractionCytoskeletal organizationCellular motilityForce generation in non-muscle cells
04

Disease associations

Cardiovascular disease (e.g., cardiomyopathies)Muscle diseases (e.g., myopathies, muscular dystrophy)Potential indirect links to cancer cell migration/invasion
05

Safety considerations

Targeting actomyosin ATPase can impair essential muscle function, leading to muscle weakness or cardiac dysfunctionNon-specific inhibition/activation can cause side effects in non-target tissues
06

Interacting drugs

Blebbistatin

4 more in the full profile.

07

Biomarkers

Myosin light chain phosphorylation statusActin-myosin cross-bridge turnover rates (indirect)Clinical: markers of cardiac or skeletal muscle damage/contractility

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