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

Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

3.4K
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...
3.4K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.1K
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,...
5.1K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K
Antihypertensive Drugs: Action of Calcium Channel Blockers01:18

Antihypertensive Drugs: Action of Calcium Channel Blockers

497
Calcium ions are essential to contract smooth muscle cells in blood vessels. They enter these cells through voltage-dependent calcium channels, specifically L-type calcium channels in the cell membrane. These L-type calcium channels are integral to the excitation-contraction coupling process in smooth muscle. When a stimulus is received by smooth muscle cells, their membrane depolarizes. This alteration in membrane potential instigates the opening of L-type calcium channels. As a result,...
497
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

2.2K
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...
2.2K
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

12.0K
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
12.0K

You might also read

Related Articles

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

Sort by
Same author

Bacillus sp. Z26 suppresses Alternaria alternata and its mycotoxins by targeting AaPex13-mediated peroxisome biogenesis.

World journal of microbiology & biotechnology·2026
Same author

Simultaneous separation of ezetimibe and its seven stereoisomers by supercritical fluid chromatography on a polysaccharide-based chiral stationary phase: Optimization and thermodynamic analysis.

Talanta·2026
Same author

Case Report: Optic nerve infiltration associated with sequential CRVO and CRAO in isolated CNS relapse of AML.

Frontiers in medicine·2026
Same author

A Simulation Study of a Bandpass Filter Formed by CNT-Core Cu-TSVs with Enhanced Thermal Management.

Micromachines·2026
Same author

Phytase modulates amino acid and mineral ion release kinetics: Ingredient-specific responses in plant protein ingredients.

Current research in food science·2026
Same author

Experience-Dependent Plasticity of Periglomerular Cells in the Olfactory Bulb.

eNeuro·2026

Related Experiment Video

Updated: Jun 25, 2025

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED
09:32

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED

Published on: May 7, 2013

19.2K

The A-kinase anchoring protein Yotiao decrease the ER calcium content by inhibiting the store operated calcium entry.

Liuqing Wang1, Jiaxuan Zhang1, Wanjie Li1

  • 1Beijing Key Laboratory of Gene Resource and Molecular Development, College of Life Sciences, Beijing Normal University, Beijing, China.

Cell Calcium
|May 23, 2024
PubMed
Summary

The Yotiao protein variant of AKAP9 reduces ER calcium levels by interacting with adenylyl cyclase 9 (AC9). This interaction suppresses calcium entry, impacting cellular calcium homeostasis.

Keywords:
Adenylyl cyclase 9ER Ca(2+) homeostasisOrai1SOCEYotiaocAMP

More Related Videos

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+
12:30

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+

Published on: May 19, 2017

14.9K
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

21.2K

Related Experiment Videos

Last Updated: Jun 25, 2025

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED
09:32

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED

Published on: May 7, 2013

19.2K
Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+
12:30

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+

Published on: May 19, 2017

14.9K
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

21.2K

Area of Science:

  • Cellular Biology
  • Molecular Mechanisms
  • Calcium Homeostasis

Background:

  • Endoplasmic reticulum (ER) calcium (Ca2+) homeostasis is crucial for cellular function and implicated in various diseases.
  • A genomic screen identified A-kinase anchoring protein 9 (AKAP9) as a regulator of ER Ca2+ levels, but its mechanism was unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which AKAP9, specifically its Yotiao variant, regulates ER Ca2+ levels.
  • To identify the key interactors involved in Yotiao's effect on ER Ca2+.

Main Methods:

  • Utilized Yotiao truncations and knock-out cells to investigate protein interactions.
  • Employed pharmacological tools to assess the role of various signaling molecules.
  • Investigated the impact of Yotiao-AC9 interaction on calcium entry.

Main Results:

  • The smallest AKAP9 splicing variant, Yotiao, was found to decrease ER Ca2+ content in animal cells.
  • Yotiao's Ca2+-lowering effect was independent of known interactors like IP3R1, PKA, PP1, and AC2.
  • Adenylyl cyclase 9 (AC9) was identified as essential for Yotiao's ER Ca2+-lowering activity.

Conclusions:

  • Yotiao, through interaction with AC9, reduces ER Ca2+ levels by suppressing store-operated calcium entry via Orai1.
  • This study reveals a novel mechanism for ER Ca2+ regulation involving the Yotiao-AC9-Orai1 axis.
  • Findings contribute to a deeper understanding of ER Ca2+ homeostasis and its dysregulation in disease.