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Hypothesis | Excitation–Contraction Coupling
D. George Stephenson
Using a mathematical model, Stephenson tests the hypothesis that the characteristic response to Ca2+ of RyR channels is key not only for the Ca2+ release mechanism in cardiac muscle and other tissues, but also for the DHPR-dependent Ca2+ release in skeletal muscles.
Methods and Approaches | Pain Focus
Taylor M. Mott, Grace C. Wulffraat, Alex J. Eddins, Ryan A. Mehl, Eric N. Senning
Mott et al. evaluate two click-chemistry protein labeling tools based on genetic code expansion technology and circularly permutated Halotag, respectively, for their utility in TRPV1 cell surface expression studies.
Article
Kristina Kooiker, Qing-Fen Gan, Ming Yu, Na Sa, Saffie Mohran, Yuanhua Cheng, Galina Flint, Stephanie Neys, Chengqian Gao, Devin Nissen, Tim McMillen, Anthony Asencio, Weikang Ma, Thomas C. Irving, Farid Moussavi-Harami, Michael Regnier
Kooiker et al. investigate the mechanisms of a novel cardiac myosin inhibitor that depends on the presence of a myosin regulatory light chain (RLC-1). They show that RLC-1 destabilizes myosin interactions to inhibit force and accelerate kinetics in cardiac muscle.
Article | Voltage-Gated Na Channels
Rita de Cássia Collaço, Filip Van Petegem, Frank Bosmans
The ω-grammotoxin-SIA peptide (GrTx-SIA) was originally found in tarantula venom and shown to inhibit voltage-gated Ca2+ channels. Here, Collaço et al. report that GrTx-SIA can also potently inhibit voltage-gated Na+ channel currents, with NaV1.6 being the most susceptible subtype.
Article
Man Si, Ahmad Darvish, Kelsey Paulhus, Praveen Kumar, Kathryn A. Hamilton, Edward Glasscock
Si et al. use electrophysiology to show that genetic or pharmacological ablation of Kv1.1 K+ channel subunits reduces the firing rate of the heart’s sinoatrial node in mice. They attribute this decrease to impaired outward K+ currents resulting in prolonged action potentials. These findings identify Kv1.1 as a novel regulator of cardiac pacemaking.
Article
Zahra Aminzare, Alan R. Kay
Animal cells regulate their volume by actively pumping sodium and potassium ions, preventing the osmotic influx of water from bursting the cell. We have extended the pump-leak equations that are used to characterize such systems to include impermeant extracellular molecules, cation–chloride co-transporters, and the energetics of ion transport.
Article
Garrett Elmore, Brooke M. Ahern, Nicholas M. McVay, Kyle W. Barker, Sarisha S. Lohano, Nemat Ali, Andrea Sebastian, Douglas A. Andres, Jonathan Satin, Bryana M. Levitan
RRAD is a constituent of the L-type calcium channel heteromultimeric complex. RRAD contributes to calcium channel modulation. Elmore, Ahern et al. show that the RRAD C-terminus confers membrane association concomitantly with the regulation of ICa,L modulation and in vivo heart function.
Issue Cover
Current Issue
Volume 156,
Issue 9,
2 September 2024
Reviews & Opinions
Commentary
Cherrie H.T. Kong, Eef Dries
Rad is an emerging key Cav1.2 modulator. In the present issue of JGP, Elmore, Ahern et al. examine how the Rad C-terminus affects its subcellular distribution and Cav1.2 regulation.
Commentary
Danuta Szczesna-Cordary
New RLC-1 small-molecule inhibits actomyosin interactions, reduces contractile force, and speeds up myosin cross-bridge kinetics.
Research News
Ben Short
JGP study reveals that, although they are present at low levels and only generate small currents in the sinoatrial node, Kv1.1 channels have a significant impact on cardiac pacemaking.

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