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ON THE COVER
Steered molecular simulation captures the pre-powerstroke to post-powerstroke transition of cardiac myosin Loop-4 along cardiac actin, initiating the translocation of tropomyosin on actin to its position on fully activated thin filaments. Image © Rynkiewicz et al., 2024. See https://doi.org/10.1085/jgp.202413538. - PDF Icon PDF LinkTable of Contents
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Articles
Myosin’s powerstroke transitions define atomic scale movement of cardiac thin filament tropomyosin
Molecular simulations by Rynkiewicz and Lehman indicate that tropomyosin repositions on thin filament actin as myosin transitions from pre-powerstroke to post-powerstroke conformation. Charge repulsion between polar residues on myosin’s Loop-4 and on individual tropomyosin pseudorepeats is shown to facilitate tropomyosin movement.
Honeybee CaV4 has distinct permeation, inactivation, and pharmacology from homologous NaV channels
Bertaud et al. characterize CaV4, a honeybee voltage-gated Ca2+ channel with high sequence homology to Na+ channels, but with a distinct permeation, voltage- and cation-dependent inactivation, and pharmacology from Na+ channels. Their study highlights the unique properties of this new class of voltage-gated Ca2+ channels.
Mutation in pore-helix modulates interplay between filter gate and Ba2+ block in a Kcv channel pore
Tewes et al. use a simple K+ channel pore to examine filter gating. Voltage-dependent closings in pore-helix mutants can be explained by an elevated sensitivity to block by trace contaminations of Ba2+. This means that the dwell time of ions in the filter determines the closed times of the filter gate.
