Newest Articles
Tetany in skeletal muscleMoss et al. highlight why high-frequency bursts at the onset of tetany increase force development in fast-twitch skeletal muscle fibers.
Doublet stimulation increases on Ca2+ and forceHigh-frequency paired stimuli used to initiate a tetanus result in increased force and rate of force development in skeletal muscle. Bakker et al. investigate this mechanism and find that doublet stimulation increases the amount of Ca2+ bound to troponin C, resulting in rapid force development.
Gating ring strengthens marriage of BK channel voltage sensing to pore openingA new JGP study shows that the gating ring helps the voltage-sensing domain open the BK channel’s pore.
Voltage-gate coupling in truncated BK channelsBoth cellular depolarization and intracellular Ca2+ can gate open large conductance Ca2+-activated K+ channels. Zhang et al. show that the intracellular gating ring, which forms the Ca2+-sensing machinery of the channel, is also required for activated voltage sensors to effectively gate open the pore.
Fusion pores and their control of exocytosisChang et al. review fusion pore structure and dynamics and discuss the implications for hormone and neurotransmitter release
The state of the community: JGP in 2017Amid a difficult year for science and scientists, The Journal of General Physiology is thriving and gearing up for its 100th anniversary celebrations.
Phasic and tonic response mechanisms in RGCsVisual stimuli of different frequencies are encoded in the retina using transient and sustained responses. Zhao et al. describe the different strategies that are used by four types of retinal ganglion cells to shape photoresponse kinetics.
Intrinsically liganded CNBhD in KCNH activationhEAG1 is a member of the KCNH family of ion channels, which are characterized by C-terminal regions with homology to cyclic nucleotide–binding domains (CNBhDs). Zhao et al. show that an “intrinsic ligand” occupying the CNBhD binding pocket promotes the activated and open state of the channel.
A missense mutation makes a mess of Ca2+ sensingA new JGP study shows how a disease-causing mutation in RyR2 dramatically alters channel behavior.
ADPR binding on TRPM2ADP ribose (ADPR) is an endogenous ligand for the transient receptor potential melastatin 2 (TRPM2) channel. Yu et al. identify 11 residues in the NUDT9 homology domain of TRPM2 that form a binding site for ADPR involving van der Waals, polar solvation, and electronic interactions.
Pages
Current Issue
June 5, 2017
Volume 149, No. 6
