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Cholesterol organization of Piezo1 channel clusters
Activation Gate Controls Inactivation

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Newest Articles

Article

| August 05 2020

Ca 2+ entry compensates for CASQ1 deficiency

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.

Article

| July 23 2020

Mechanism of calcium potentiation of the α7 nicotinic acetylcholine receptor

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.

Article

| July 07 2020

A rational mutation to investigate HCN channels in vivo

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.

Article

| June 26 2020

Functional heterogeneity in STIM1-Orai1 puncta

Joseph L. Dynes, Andriy V. Yeromin, Michael D. Cahalan

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.

Article

| June 24 2020

Cholesterol organization of Piezo1 channel clusters

Pietro Ridone, Elvis Pandzic, Massimo Vassalli, Charles D. Cox, Alexander Macmillan, Philip A. Gottlieb, Boris Martinac

The essential mammalian mechanosensitive channel PIEZO1 organizes in the plasma membrane into nanometric clusters that depend on the integrity of cholesterol domains to rapidly detect applied force and especially inactivate synchronously, the most commonly altered feature of PIEZO1 in pathology.

Article

| June 22 2020

The E1784K mutant in Nav1.5 disrupts inactivation through two mechanisms

Colin H. Peters, Abeline R. Watkins, Olivia L. Poirier, Peter C. Ruben

Inheritable and de novo variants of voltage-gated sodium channels that lead to sudden cardiac death can affect several different aspects of channel function, making pharmaceutical treatment difficult. Peters et al. show that the E1784K mutant in Nav1.5 alters channel function through two distinct and separable mechanisms.

Article

| June 19 2020

Complex Zn 2+ effects on Ca v 2.3 channel function

Felix Neumaier, Serdar Alpdogan, Jürgen Hescheler, Toni Schneider

Neumaier et al. reveal that Zn2+ effects on Cav2.3 channels are complex, can be either inhibitory or stimulatory, and may persist for several minutes after cessation of the Zn2+ signal. A Markov model is developed that can account for Cav2.3 channel currents in the absence and presence of physiological Zn2+ concentrations.

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August 3, 2020

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Reviews & Opinions

Viewpoint

| July 28 2020

SNAP25, exocytosis, fusion pore, dynamic acceptor complex

Ronald W. Holz, Mary A. Bittner

The domain in SNAP25 that links its two SNARE motifs plays important roles in fusion pore formation, secretion kinetics, and the formation of a dynamic plasma membrane SNAP25/syntaxin “acceptor” complex for the v-SNARE synaptobrevin.

Research News

| July 15 2020

Cholesterol helps PIEZO1 use the force

Ben Short

JGP study shows that disruption of membrane cholesterol alters the organization and activity of mechanosensitive PIEZO1 channels.

Commentary

| June 24 2020

An ion channel in the company of a transporter

Eric Accili

In the current issue of JGP, Lamothe and Kurata explore the functional relationship between the Kv1.2 potassium channel, with Kvβ1.2 bound to the interior aspect of the channel, and Slc7a5, a component of the neutral amino acid transporter LAT1.

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Ion Channel Structure and Function

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All articles temporarily free to read. Learn about the steps we're taking and find COVID-19 relevant content.

Submit your research by September 30, 2020 to be considered for a special issue edited by Christine Cremo, Henk Granzier, and Richard L. Moss. Learn more

Quickly see whether citations provide supporting or disputing evidence for the cited claim directly in the article metrics section. Learn more

Cholesterol organization of Piezo1 channel clusters

Activation Gate Controls Inactivation

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