Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
Sometimes a single EPSP is strong enough to induce an action potential in the postsynaptic neuron. However, multiple presynaptic inputs must often create EPSPs around the same time for the postsynaptic neuron to be sufficiently depolarized to fire an action potential.
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Multiscale imaging of basal cell dynamics in the functionally mature mammary gland.

Proceedings of the National Academy of Sciences of the United States of America·2020
Same author

A calcium/cAMP signaling loop at the ORAI1 mouth drives channel inactivation to shape NFAT induction.

Nature communications·2019
Same author

Store-operated Ca<sup>2+</sup> entry and Ca<sup>2+</sup> responses to hypothalamic releasing hormones in anterior pituitary cells from Orai1-/- and heptaTRPC knockout mice.

Biochimica et biophysica acta. Molecular cell research·2018
Same author

A personal journey.

Cell calcium·2018
Same author

Store-Operated Calcium Entry: An Historical Overview.

Advances in experimental medicine and biology·2018
Same author

Orai1 Plays a Crucial Role in Central Sensitization by Modulating Neuronal Excitability.

The Journal of neuroscience : the official journal of the Society for Neuroscience·2017

Related Experiment Video

Updated: Jul 15, 2026

Applications of Spatio-temporal Mapping and Particle Analysis Techniques to Quantify Intracellular Ca2+ Signaling In Situ
09:34

Applications of Spatio-temporal Mapping and Particle Analysis Techniques to Quantify Intracellular Ca2+ Signaling In Situ

Published on: January 7, 2019

New molecular players in capacitative Ca2+ entry.

James W Putney1

  • 1National Institute of Environmental Health Sciences - NIH, PO Box 12233, Research Triangle Park, NC 27709, USA. putney@niehs.nih.gov

Journal of Cell Science
|May 5, 2007
PubMed
Summary

Capacitative calcium entry (CCE) is activated by Stim1, an ER calcium sensor. Stim1 signals to Orai proteins in the plasma membrane, which form the pores of store-operated calcium channels.

Area of Science:

  • Cell Biology
  • Molecular Physiology
  • Calcium Signaling

Background:

  • Capacitative calcium entry (CCE) links intracellular calcium store depletion to plasma membrane calcium channel activation.
  • For twenty years, the mechanisms and components of CCE, including Transient Receptor Potential (TRP) channels, have been investigated.
  • Recent discoveries have identified key molecular players in CCE.

Purpose of the Study:

  • To elucidate the roles of Stim1 and Orai proteins in the signaling and permeation of store-operated calcium channels.
  • To understand the spatial dynamics of Stim1 during CCE.
  • To confirm Orai proteins as the pore-forming subunits of store-operated channels.

Main Methods:

  • The study focuses on the molecular mechanisms of capacitative calcium entry.

More Related Videos

Single-Cell Calcium Imaging for Studying the Activation of Calcium Ion Channels
07:17

Single-Cell Calcium Imaging for Studying the Activation of Calcium Ion Channels

Published on: December 13, 2024

Methods for Cell-attached Capacitance Measurements in Mouse Adrenal Chromaffin Cell
08:24

Methods for Cell-attached Capacitance Measurements in Mouse Adrenal Chromaffin Cell

Published on: October 22, 2014

Related Experiment Videos

Last Updated: Jul 15, 2026

Applications of Spatio-temporal Mapping and Particle Analysis Techniques to Quantify Intracellular Ca2+ Signaling In Situ
09:34

Applications of Spatio-temporal Mapping and Particle Analysis Techniques to Quantify Intracellular Ca2+ Signaling In Situ

Published on: January 7, 2019

Single-Cell Calcium Imaging for Studying the Activation of Calcium Ion Channels
07:17

Single-Cell Calcium Imaging for Studying the Activation of Calcium Ion Channels

Published on: December 13, 2024

Methods for Cell-attached Capacitance Measurements in Mouse Adrenal Chromaffin Cell
08:24

Methods for Cell-attached Capacitance Measurements in Mouse Adrenal Chromaffin Cell

Published on: October 22, 2014

  • Investigates the function and localization of Stim1 and Orai proteins.
  • Utilizes concepts from cell biology and molecular physiology to analyze calcium signaling pathways.
  • Main Results:

    • Stim1 acts as an endoplasmic reticulum calcium sensor.
    • Stim1 redistributes within the ER to approach the plasma membrane but does not translocate into it.
    • Stim1 directly signals to Orai proteins, which are identified as the pore-forming subunits of store-operated channels.

    Conclusions:

    • Stim1 and Orai proteins are crucial components of the store-operated calcium channel complex.
    • Stim1's redistribution within the ER is a key signaling event for channel activation.
    • Orai proteins form the actual calcium-permeable pores of these channels, validating their role in CCE.