Newest Articles
F88L in TnT attenuates length-dependent activationThe F88L mutation in cardiac troponin T (TnTF88L) is associated with hypertrophic cardiomyopathy. Reda and Chandra reveal that it abolishes length-mediated increase in myofilament Ca2+ sensitivity and attenuates cooperative mechanisms governing length-dependent activation.
Functional characterization of purified SthK channelsSthK is a bacterial cyclic nucleotide–gated ion channel from Spirochaeta thermophila. By optimizing the expression and purification of SthK, Schmidpeter et al. show that cAMP and cGMP bind to the channel with similar affinity but activate it with different efficacy.
A snail proton channel with anomalous propertiesVoltage-gated proton currents were first discovered in snail neurons. Thomas et al. identify a snail proton channel gene that codes for a rapidly activating proton channel that differs from other proton channels, in particular by its low sensitivity to intracellular pH.
His168 is an internal pH sensor of hHV1Voltage-gated proton channels open appropriately in myriad physiological situations because their gating is powerfully modulated by both pHo and pHi. Cherny et al. serendipitously identify a histidine at the inner end of the S3 helix that is required for the response to pHi.
Cypher regulates CaV1.2 calcium channelA-kinase anchoring proteins are required for β-adrenergic stimulation of L-type Ca2+ channels in cardiac myocytes, but the molecular species that is responsible for this regulation remains unknown. Yu et al. reveal that Cypher/Zasp is a key regulator of β-adrenergic regulation in cardiac myocytes.
Zn2+-dependent conformational coupling in Hv1Hv1 proteins form a voltage-gated proton channel that is inhibited by extracellular Zn2+. De La Rosa et al find that extracellular Zn2+ is octahedrally coordinated by specific protein atoms and that Zn2+ occupancy modulates voltage sensor activation in Hv1 by long-range conformational coupling to a conserved intracellular electrostatic network.
Ligand-induced structural rearrangements in TRPA1TRPA1 channels transduce chemical, inflammatory, and neuropathic pain and are modulated by both electrophilic and nonelectrophilic compounds. Samanta et al. show that these modulators cause conformational rearrangements in the N-terminal ankyrin repeats, the pre-S1 helix, the TRP-like domain, and the linkers region of the channel.
Current Issue
May 7, 2018
Volume 150, No. 5
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Reviews & Opinions
- Influences: Cold Spring Harbor summer courses and Drosophila melanogaster neurogenetics
The Jans recollect features of the scientific environments that influenced their careers.
- Membrane-mediated interaction drives mitochondrial ATPase assembly and cristae formation
Cui reflects on new coarse-grained simulations demonstrating that mitochondrial ATP synthase dimers spontaneously self-associate.
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JGP paper presents a model for studying cyclic nucleotide–modulated channels.