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Cover Image
Cover Image
ON THE COVER
Membrane ridge formed by four mitochondrial ATP synthase dimers, based on coarse-grained MD simulations. Each of the dimers is colored differently. The membrane surface is shown in gray. The dimers are driven together by a long-range membrane-induced force to minimize the overall strain of the lipid bilayer that is caused by the unusual V-like shape of each dimer. Ridges comprising tens of dimers over hundreds of nanometers enable the inner mitochondrial membrane to develop its characteristic invaginations, known as cristae.
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Research News
Deafness-associated mutation opens the gate to understanding
New JGP study uncovers a connection between Connexin 26 fast and slow gates.
Essay
Influences: Childhood, boyhood, and youth
Miller recounts the distinct influences that Gilbert Ling and Efraim Racker had on his early career.
Review
Cryo-electron microscopy structures and progress toward a dynamic understanding of KATP channels
Puljung reviews recent cryo-EM KATP channel structures and proposes a mechanism by which ligand binding results in channel opening.
Viewpoint
The ins and outs of vesicular monoamine transporters
Yaffe et al. review structure-guided studies that have provided insight into the mechanism of proton-monoamine antiport by VMATs.
Article
Dimerization of the voltage-sensing phosphatase controls its voltage-sensing and catalytic activity
The Ciona intestinalis voltage-sensing phosphatase (Ci-VSP) was not thought to multimerize. Rayaprolu et al. show that Ci-VSP exists as a dimer and that this interaction lowers the voltage dependence of activation and alters substrate specificity.
The syndromic deafness mutation G12R impairs fast and slow gating in Cx26 hemichannels
Mutations in connexin 26 hemichannels that cause syndromic deafness have a gain-of-function phenotype that is poorly understood. García et al. show that one such mutation impairs fast and slow gating in these hemichannels because of an interaction between the N terminus and intracellular loop.
Full and partial agonists evoke distinct structural changes in opening the muscle acetylcholine receptor channel
Different agonists activate the muscle AChR with different efficacies. Mukhtasimova and Sine show that oxidative cross-linking of proximal residues alters the ability of some agonists but not others to open the AChR channel. The findings show that, in opening the channel, agonists with differing efficacy elicit distinct structural changes.
Atom-by-atom tuning of the electrostatic potassium-channel modulator dehydroabietic acid
Dehydroabietic acid was recently shown to open voltage-gated potassium channels. Silverå Ejneby et al. show that its effect peaks when the carboxyl-group charge and hydrophobic anchor are separated by three atoms and use this rule to design molecules that open the human Kv7.2/7.3 potassium channel.
Structural insights into the molecular mechanism of mouse TRPA1 activation and inhibition
TRPA1 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.
Communication
Mitochondrial ATP synthase dimers spontaneously associate due to a long-range membrane-induced force
Rows of ATP synthase dimers define the cristae morphology of the inner mitochondrial membrane. Anselmi et al. use molecular simulations to show that the formation of these rows is spontaneous and driven by an attractive force induced by the membrane, not direct protein–protein interactions.
