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Posttranslational modifications in microtubules affect cytoskeletal mechanics and mechanotransduction. In this study, Coleman et al. show that acetylated α-tubulin affects cytoskeletal stiffness and viscoelastic resistance, thus revealing another regulator of striated muscle mechanotransduction.

Fazlollahi et al. show that contraction and relaxation remain tightly coupled in intact canine myocardium after exercise training and/or myocardial infarction. They postulate that the action of cardiac myosin binding protein C on actin and myosin may play a key role in this process.


Stronczek et al. analyze the structure of the titin-N2A poly-Ig segment, a key signaling element in the sarcomere. They reveal a unique topography for the I81-I83 tandem, but they could not confirm the presence of Ca2+ binding sites in I81-I83 or the interaction of N2A with actin.

Cardiac myosin-binding protein C (cMyBP-C) is thought to regulate cardiac muscle and heart contraction. Hanft et al. show that cMyBP-C phosphorylation regulates length dependence of power output in murine permeabilized cardiac myocytes, which translates to in vivo Frank–Starling relationships.

Mamidi et al. investigate the effect of cardiac myosin-binding protein C (cMyBPC) phosphorylation on the response to omecamtiv mecarbil (OM), a candidate heart failure therapy. They show that OM uncouples myocardial force dynamics from cMyBPC phosphorylation, suggesting important therapeutic constraints.


This review focuses on thin filament regulatory mechanisms with emphasis on cardiac-specific mechanisms in the three-state model of sarcomere activation and on signaling cascades at the barbed and pointed ends.

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