Newest Articles
Different agonists evoke distinct structural changesDifferent 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.
The vesicular monoamine transportersYaffe et al. review structure-guided studies that have provided insight into the mechanism of proton-monoamine antiport by VMATs.
Membrane force drives ATP synthase dimers to form rowsRows 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.
Altered fast and slow gating elicited by Cx26G12RMutations 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.
Tuning of a potassium-channel modulatorDehydroabietic 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.
Functional anatomy of CFTRHwang et al. integrate new structural insights with prior functional studies to reveal the functional anatomy of CFTR chloride channels.
Role of intrinsic ligand in KCNH channelsKhoo and Pless examine new work that provides mechanistic insight into the role of the intrinsic ligand in KCNH ion channels.
Intrinsic ligand regulates KCNH channelsKCNH potassium channels possess an intrinsic ligand in their cyclic nucleotide-binding homology domain, located at the N- and C-terminal domain interface. Dai et al. show that this intrinsic ligand regulates voltage-dependent potentiation via a rearrangement between the ligand and its binding site.
Influences: Short circuitsClapham recalls his early adventures with Lou DeFelice and Erwin Neher.
Endocytosis restores release at ribbon synapsesIn addition to recycling vesicles, synaptic endocytosis restores release site competence after exocytosis. Wen et al. show that endocytosis is essential for subsequent fusion but not docking of vesicles at photoreceptor ribbon synapses and for maintaining release at modest frequencies.
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Current Issue
June 4, 2018
Volume 150, No. 6
