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Muhammad Umair Naseem, Edson Carcamo-Noriega, José Beltrán-Vidal, Jesus Borrego, Tibor G. Szanto, Fernando Z. Zamudio, Gustavo Delgado-Prudencio, Lourival D. Possani, Gyorgy Panyi
Naseem et al. show that the Cm28 peptide found in scorpion venom is a potent inhibitor of the KV1.2 and KV1.3 K+ channels. Cm28 is a pore blocker that obeys a unique primary structure with only 27 amino acid residues and the lack of the functional dyad characteristic of other α-KTx peptides.
José J. De Jesús-Pérez, Ana E. López-Romero, Odalys Posadas, Guadalupe Segura-Covarrubias, Iván Aréchiga-Figueroa, Braulio Gutiérrez-Medina, Patricia Pérez-Cornejo, Jorge Arreola
De Jesús-Pérez et al. show that a reciprocal regulation between key gating elements and permeant anions sets the calcium and voltage sensitivities and the anion selectivity of the calcium-activated chloride channel TMEM16A.
Kerri Spontarelli, Daniel T. Infield, Hang N. Nielsen, Rikke Holm, Victoria C. Young, Jason D. Galpin, Christopher A. Ahern, Bente Vilsen, Pablo Artigas
Spontarelli et al. show that Y780, a disease-relevant residue in the sodium pump’s sodium-exclusive ion-binding site, stabilizes sodium binding there through a hydrogen bond, without the participation of cation–π interactions and controls K+ interaction at the other two ion-binding sites indirectly through a hydrogen-bond network.
Niklas Brake, Adamo S. Mancino, Yuhao Yan, Takushi Shimomura, Yoshihiro Kubo, Anmar Khadra, Derek Bowie
Combining electrophysiology and kinetic modeling, Brake et al. highlight the role of closed-state inactivation in the gating behavior of cardiac, skeletal muscle, and neuronal voltage-gated sodium channels.
Nicole E. Godellas, Claudio Grosman
Godellas and Grosman revisit the use of ligand-binding assays to study pentameric ligand-gated ion channels (pLGICs). They show that ligand-binding affinity is unaffected by binding-site occupancy and that changes to the transmembrane domain are unlikely to affect binding to the extracellular domain.
Robert C. Klipp, John R. Bankston
Arachidonic acid (AA) is a known modulator of ASICs. Klipp and Bankston examine the structural requirements for ASIC modulation by a number of lipids related to AA. Negatively charged head groups are stronger potentiators and may interact with an arginine in TM1 near the outer leaflet of the plasma membrane.
Klaus Benndorf, Thomas Eick, Christian Sattler, Ralf Schmauder, Eckhard Schulz
Benndorf et al. present a strategy to analyze the functionality of heteromeric ligand-gated ion channels by combining subunit concatenation, mutagenesis, and extensive global fit strategies with intimately coupled Markov models.

Related Articles from Rockefeller University Press

Issue Cover
Current Issue
Volume 154,
Issue 6,
6 June 2022
Reviews & Opinions
Viewpoint | Excitation–Contraction Coupling
Samantha C. Salvage, Christopher L.-H. Huang, James A. Fraser, Angela F. Dulhunty
The promiscuity of flecainide underscores its antiarrhythmic efficacy in CPVT: this paper presents a discussion of its mechanisms of action on the cardiac ryanodine receptor (RyR2) and other cardiac excitation–contraction coupling proteins.
Research News
Ben Short
JGP study uses both natural and unnatural amino acid substitutions to examine how a key tyrosine residue controls the selectivity of the Na+/K+ pump.
Commentary | Excitation–Contraction Coupling
Werner Melzer
Melzer discusses a recent JGP study showing that alternative splicing of the skeletal muscle L-type calcium channel impacts on a modulatory effect of its γ subunit.

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