Journal of General Physiology | Rockefeller University Press

Time 2020-09-17 03:02:41

Web Name: Journal of General Physiology | Rockefeller University Press

WebSite: http://jgp.rupress.org

ID:49360

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JGP staff members are working remotely in line with New York City s efforts to contain COVID-19. While our offices are physically closed, editorial and publication operations continue. JGP staff can be reached via email and phone, as we tend to our family, friends and community. Thank you for your patience and understanding.Our pilot partnership with Society of General Physiologists offers a $500 discount to members on our $2,000 publication fee. Learn more about SGP membership. Vladimir V. Cherny, Boris Musset, Deri Morgan, Sarah Thomas, Susan M.E. Smith, Thomas E. DeCoursey The voltage-gated proton channel (HV1) resembles the voltage sensors of other channels, but its movement during channel opening remains controversial. Cherny et al. establish open and closed gating configurations of HV1 by analyzing the interactions of Zn2+ with an introduced histidine residue. K+ binding to mammalian glutamate transporters is essential for the import and release of glutamate into cells. Using MD simulations and site-directed mutagenesis, Wang et al. identify two K+ binding sites in the transporter EAAC1, one of which appears to catalyze the relocation step of the transport cycle. Maria A. Neginskaya, Jasiel O. Strubbe, Giuseppe F. Amodeo, Benjamin A. West, Shoshana Yakar, Jason N. Bazil, Evgeny V. Pavlov Stress increases the permeability of the mitochondrial inner membrane by activating permeability transition pores (PTPs), likely composed of ATP synthase or the adenine nucleotide translocator. By measuring water flux during calcium-activated mitochondrial swelling, Neginskaya et al. estimate that if these proteins are involved in PTP, only a small fraction becomes transformed into the pore on a single mitochondrion. Antonio Michelucci, Simona Boncompagni, Laura Pietrangelo, Takahiro Takano, Feliciano Protasi, Robert T. Dirksen, Robert T. Dirksen Mice lacking calsequestrin-1 have reduced levels of releasable Ca2+ in the sarcoplasmic reticulum of their skeletal muscles. Michelucci et al. reveal that this is compensated by constitutive assembly of STIM1 and Orai1 into Ca2+ entry units, promoting both constitutive and store-operated Ca2+ entry. Kathiresan Natarajan, Nuriya Mukhtasimova, Jeremías Corradi, Matías Lasala, Cecilia Bouzat, Steven M. Sine The α7 nicotinic acetylcholine receptor (nAChR) is highly abundant in the brain but is frequently located at extra-synaptic regions where the concentration of ACh is low. Natarajan et al. reveal that at low ACh concentrations, calcium potentiates α7 channel opening by binding to a novel structural motif. Alessandro Porro, Anna Binda, Matteo Pisoni, Chiara Donadoni, Ilaria Rivolta, Andrea Saponaro The gating of neuronal HCN channels is modulated by the competitive binding of cAMP and TRIP8b, a brain-specific protein that also controls channel trafficking. Porro et al. identify a rational mutation in HCN channels that affects binding of TRIP8b, without altering cAMP affinity or TRIP8b-dependent trafficking. The mutation represents a valuable tool to investigate HCN channels in vivo. The authors use a fluorescent genetically encoded Ca2+ indicator, GCaMP6f, fused to Orai1 to visualize Ca2+ influx through store-operated Orai1 channels. Combined with whole-cell recording of transfected human cells, this reporter reveals heterogeneity of channel activation and kinetics in STIM1-Orai1 puncta within the same cell.Subscribe to RSS headline updates from: Powered by FeedBurner Cherny and coworkers use zinc ion as a probe to identify different conformational states of voltage-gated proton (Hv1) channels. Agonist actions at transition states can explain the observation that different pathways are taken for acetylcholine receptor desensitization and recovery. In this issue, Michelucci et al. report the existence of specific sites acting as Ca2+ entry units (CEUs) in fast skeletal muscle of mice lacking calsequestrin (CASQ1), the major Ca2+ binding protein of the SR. The CEU provides constitutive and store-operated Ca2+ entry (SOCE) and resistance to force decline resulting from SR Ca2+ depletion during repetitive muscle activity. This site uses cookies. By continuing to use our website, you are agreeing to our privacy policy.

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Journal of General Physiology (JGP) publishes mechanistic and quantitative cellular and molecular physiology of the highest quality. Est. 1918

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