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Cover Image
Cover Image
Cover picture: Image of quantum dot–labeled myosin light chain kinase (MLCK) molecules (green) colocalized on actin (red) in the stress fibers of a permeabilized human airway smooth muscle cell. MLCK molecules move along actin in a sustained manner by a random diffusion mechanism. ATP and Ca2+-calmodulin strongly promote this movement, suggesting that MLCK diffusion on actin is a mechanism to enhance the rate of myosin phosphorylation during muscle activation (see Research article by Hong et al., 267–280).
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Generally Physiological
Article
Diffusion of myosin light chain kinase on actin: A mechanism to enhance myosin phosphorylation rates in smooth muscle
One-dimensional diffusion of myosin light chain kinase along actin filaments enables the rapid phosphorylation of smooth muscle myosin.
Na,K-ATPase α2 activity in mammalian skeletal muscle T-tubules is acutely stimulated by extracellular K+
The K+ affinity of the Na,K-ATPase α2 isoform matches its activity to the range of extracellular K+ concentrations in the T-tubules at rest and during contraction, maintaining the excitability of active muscle.
Reconciling depressed Ca2+ sparks occurrence with enhanced RyR2 activity in failing mice cardiomyocytes
Alterations in the intracellular environment lead to decreased frequency of Ca2+ sparks in a model of heart failure despite enhanced ryanodine receptor activity.
A novel Ca2+-feedback mechanism extends the operating range of mammalian rods to brighter light
A previously unidentified calcium-dependent mechanism contributes to light adaptation in mammalian rods.
A chimeric prokaryotic pentameric ligand–gated channel reveals distinct pathways of activation
A chimeric ligand–gated channel is activated by the ligands that activate both parent channels, which gate it through two distinct mechanisms.
