Mutations D166V (HCM) and A57G (HCM) in myosin light chains destabilize the energy-conserving SRX state, shifting myosin heads toward the DRX state and causing hypercontractility; while D94A (DCM) and E143K (RCM) mutations stabilize the SRX state, correlating with hypocontractility and impaired cardiac function in mouse models.
Does modulating the myosin super-relaxed state improve cardiac phenotypes in mouse models of myosin light chain-linked cardiomyopathies?
Mutation-induced dysregulation of the myosin super-relaxed state is a central mechanism driving distinct cardiomyopathy phenotypes, highlighting the SRX-DRX balance as a promising therapeutic target.
Abstract In this review, we summarize a series of studies focused on cardiac myosin light chains and hereditary human mutations that cause hypertrophic (HCM), restrictive (RCM), or dilated (DCM) cardiomyopathy. In the heart, myosin serves as the molecular motor that converts the chemical energy of ATP hydrolysis into mechanical force, enabling cardiac contraction and blood pumping. Both myosin light chains, the regulatory (RLC) and essential (ELC), play critical roles in supporting and fine-tuning myosin motor function. Special emphasis is placed on the myosin super-relaxed (SRX) state, first described by Roger Cooke and colleagues more than 15 years ago. During diastole and muscle relaxation, myosin heads dynamically transition between two energetic states: the SRX state, which minimizes ATP consumption and preserves energy, and the disordered relaxed (DRX) state, in which myosin heads are more available for actin interaction but exhibit higher ATP turnover. To elucidate mechanisms underlying mutation-dependent pathological cardiac remodeling, we assessed the relative occupancy of myosin heads between the SRX and DRX states in skinned cardiac fibers from mouse models of HCM, RCM, and DCM using single-nucleotide turnover assays developed by the Cooke laboratory. Collectively, these studies demonstrate that mutation-induced alterations in myosin energetic states and dysregulation of the SRX:DRX balance constitute a central mechanism driving the distinct clinical and functional phenotypes observed in human cardiomyopathies caused by mutations in myosin RLC and ELC.
Danuta Szczesna‐Cordary (Mon,) conducted a review in Mouse models of hypertrophic, restrictive, and dilated cardiomyopathy carrying mutations in myosin regulatory light chain (MYL2 gene) and essential light chain (MYL3 gene). Genetic mutations in myosin light chains (RLC and ELC), including D166V, D94A, A57G, E143K, and Δ43 truncation vs. Wild-type myosin light chains in otherwise genetically identical mouse models was evaluated on Distribution of myosin cross-bridges between the super-relaxed (SRX) and disordered relaxed (DRX) states and cardiac phenotypic remodeling including hypertrophy, fibrosis, contractile function. Mutations D166V (HCM) and A57G (HCM) in myosin light chains destabilize the energy-conserving SRX state, shifting myosin heads toward the DRX state and causing hypercontractility; while D94A (DCM) and E143K (RCM) mutations stabilize the SRX state, correlating with hypocontractility and impaired cardiac function in mouse models.