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

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

7.0K
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,...
7.0K
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

4.2K
Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
4.2K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

8.0K
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...
8.0K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

4.1K
4.1K
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

12.8K
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...
12.8K
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

5.8K
5.8K

You might also read

Related Articles

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

Sort by
Same author

Comparative study of triple intravenous chemotherapy versus dual chemotherapy combined with hepatic arterial infusion in patients with liver metastases from colorectal cancer.

Frontiers in oncology·2026
Same author

Blood-Brain Barrier (BBB)-Penetrable Androgen Receptor (AR) Degrader as a Potential Therapeutic Agent for Glioblastoma.

ACS pharmacology & translational science·2026
Same author

MicroRNA profiles in colostrum and transition milk of non-dairy goats fed with or without resveratrol.

Scientific data·2026
Same author

Integrated transcriptomic and metabolomic analyses elucidate the molecular mechanisms underlying quality formation during Rosa acicularis fruit ripening.

Food research international (Ottawa, Ont.)·2026
Same author

Lake Water Depth and Nutrient Gradients Mediate Aquatic Plant Distribution via the Strength of Trait Network Associations.

Global change biology·2026
Same author

The Dianthus spiculifolius chlorophyll-binding protein DsSep2 can be used as a genetic resource to create 'golden leaf' plants.

Journal of plant physiology·2026

Related Experiment Video

Updated: Mar 20, 2026

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

2.1K

TMCO1 Is an ER Ca(2+) Load-Activated Ca(2+) Channel.

Qiao-Chu Wang1, Qiaoxia Zheng1, Haiyan Tan2

  • 1State Key Laboratory of Membrane Biology, Institute of Zoology, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing 100101, China.

Cell
|May 24, 2016
PubMed
Summary

The endoplasmic reticulum (ER) protein TMCO1 acts as a calcium load-activated calcium channel (CLAC), preventing ER calcium stores from overfilling. This discovery offers insights into cellular calcium homeostasis and related developmental disorders.

More Related Videos

Fluorescence-based Measurement of Store-operated Calcium Entry in Live Cells: from Cultured Cancer Cell to Skeletal Muscle Fiber
14:18

Fluorescence-based Measurement of Store-operated Calcium Entry in Live Cells: from Cultured Cancer Cell to Skeletal Muscle Fiber

Published on: February 13, 2012

21.9K
Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

10.1K

Related Experiment Videos

Last Updated: Mar 20, 2026

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

2.1K
Fluorescence-based Measurement of Store-operated Calcium Entry in Live Cells: from Cultured Cancer Cell to Skeletal Muscle Fiber
14:18

Fluorescence-based Measurement of Store-operated Calcium Entry in Live Cells: from Cultured Cancer Cell to Skeletal Muscle Fiber

Published on: February 13, 2012

21.9K
Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
08:27

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

10.1K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Maintaining calcium (Ca2+) homeostasis in the endoplasmic reticulum (ER) is vital for cellular signaling and function.
  • The Ca2+-release-activated Ca2+ (CRAC) channel refills ER stores, but mechanisms preventing ER Ca2+ overload are unknown.

Purpose of the Study:

  • To investigate the role of TMCO1 in regulating ER Ca2+ levels.
  • To characterize TMCO1 as a potential Ca2+ channel involved in preventing ER Ca2+ overload.

Main Methods:

  • Studied TMCO1's function in ER Ca2+ regulation.
  • Investigated TMCO1's oligomerization state in response to Ca2+ levels.
  • Reconstituted TMCO1 channel activity in giant liposomes.
  • Examined TMCO1 function in knockout mouse models.

Main Results:

  • TMCO1 is an ER transmembrane protein that prevents ER Ca2+ stores from overfilling.
  • TMCO1 functions as a Ca2+ load-activated Ca2+ channel (CLAC).
  • TMCO1 undergoes reversible tetramerization upon ER Ca2+ overload and disassembles upon depletion.
  • TMCO1 knockout mice exhibit ER Ca2+ mishandling and features of cerebrofaciothoracic dysplasia spectrum.

Conclusions:

  • TMCO1 acts as a crucial protective mechanism against ER Ca2+ overfilling.
  • TMCO1 dysfunction is linked to cerebrofaciothoracic dysplasia spectrum disorders.
  • TMCO1 represents a novel target for understanding and treating Ca2+ dysregulation disorders.