Key result
Full-length myosin light chain kinase bound to stress fibers and was not dissociated by Ca2+/calmodulin, yet remained sufficient for Ca2+-dependent phosphorylation and contraction.
Population
Smooth muscle-derived A7r5 cells
Comparison
Expression of full-length myosin light chain… vs Truncated kinase vs full-length kinase
Design
Preclinical
Authors
Loading...
Challenges necessity of MLCK dissociation for myosin phosphorylation; extends molecular models but leaves open cardiac myocyte relevance.
Dissociation of myosin light chain kinase from actin-containing thin filaments is not necessary for phosphorylation of myosin light chain in thick filaments.
Lin et al. (1999) studied this question. Full-length myosin light chain kinase vs. Truncation mutant lacking residues 2-142 was evaluated on Binding properties to stress fibers and dissociation by Ca2+/calmodulin. Full-length myosin light chain kinase bound to stress fibers and was not dissociated by Ca2+/calmodulin, yet remained sufficient for Ca2+-dependent phosphorylation and contraction.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: