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Cover Image
Cover Image
Cover picture: Structural model of Xenopus α1/β3 Na+/K+ pump, based on dogfish Na+/K+-ATPase (Protein Data Bank accession no. 2ZXE; Shinoda et al. 2009. Nature. 459:446–450), with α (grey, with colored transmembrane helices), β (green surface), and γ (red helix) subunits. The Na+/K+ pump is found to be a hybrid transporter that mediates proton import during Na+/K+ exchange, and the proton route is identified. See Vedovato and Gadsby (449–464) and Hilgemann (437–441).
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Generally Physiological
Review
Commentary
Article
Route, mechanism, and implications of proton import during Na+/K+ exchange by native Na+/K+-ATPase pumps
The Na+/K+ pump is a hybrid transporter that can also import protons at physiological K+ and Na+ concentrations.
Differential Cav2.1 and Cav2.3 channel inhibition by baclofen and α-conotoxin Vc1.1 via GABAB receptor activation
The analgesic α-conotoxin Vc1.1 inhibits Cav2.3 channels through a GABAB receptor–dependent pathway involving c-Src.
Mechanotransduction and hyperpolarization-activated currents contribute to spontaneous activity in mouse vestibular ganglion neurons
Ex vivo analyses indicate that spontaneous activity in vestibular neurons depends on resting hair cell mechanotransduction and HCN channels in calyx terminals.
Stoichiometry of altered hERG1 channel gating by small molecule activators
Agonists bind to sites on all four subunits to activate human ether-a-go-go–related gene 1 (hERG1) K+ channels.
Methods and Approaches
Sarcomere length nanometry in rat neonatal cardiomyocytes expressed with α-actinin–AcGFP in Z discs
Nanoscale imaging of cultured cardiomyocytes allows the quantitative assessment of changes in the length of single sarcomeres during contractile events.
