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

6.0K
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,...
6.0K
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

16.5K
Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
16.5K
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

9.3K
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
9.3K
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

3.8K
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...
3.8K
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

14.2K
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...
14.2K
Postsynaptic Potential (PSP)01:32

Postsynaptic Potential (PSP)

4.8K
Postsynaptic potential (PSP) refers to a change in the electrical potential of a neuron when neurotransmitters released by presynaptic neurons bind to postsynaptic receptors. This potential can either be excitatory, leading to depolarization and ultimately action potential generation, or inhibitory, leading to hyperpolarization and suppression of the postsynaptic neuron.
There are two types of receptors: ionotropic and metabotropic.
The ionotropic receptor is the membrane protein that has an...
4.8K

You might also read

Related Articles

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

Sort by
Same author

Author Correction: Spinal cord Tau pathology induces tactile deficits and cognitive impairment in Alzheimer's disease via dysregulation of CCK neurons.

Nature neuroscience·2026
Same author

Two Molecularly Defined Neuronal Types in the Mammillary Body Govern Different Temporal Periods during Working Memory Maintenance.

Research (Washington, D.C.)·2026
Same author

The schizophrenia associated protein DISC1 forms a multivalent tetrameric hub via conserved UVR dimers.

Nature communications·2026
Same author

Molecular insights into Candida auris glycosylphosphatidylinositol transamidase.

Protein & cell·2026
Same author

CDKL5 modulates the plasticity of excitatory synapses via liquid-liquid phase separation.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Molecular basis of collagen galactosylation by GLT25D1.

Nature communications·2026

Related Experiment Video

Updated: Jan 14, 2026

Electroconvulsive Seizures in Rats and Fractionation of Their Hippocampi to Examine Seizure-induced Changes in Postsynaptic Density Proteins
09:07

Electroconvulsive Seizures in Rats and Fractionation of Their Hippocampi to Examine Seizure-induced Changes in Postsynaptic Density Proteins

Published on: August 15, 2017

12.6K

IQSEC2/BRAG1 may modulate postsynaptic density assembly through Ca2+-induced phase separation.

Guanhua Bai1, Ruifeng Huang1, Xinyue Nan2,3

  • 1School of Life Sciences, Southern University of Science and Technology , Shenzhen, China.

The Journal of Cell Biology
|October 22, 2025
PubMed
Summary
This summary is machine-generated.

IQSEC2 protein orchestrates synapse assembly through calcium-triggered phase separation. Dysregulation of this process may contribute to neurodevelopmental disorders related to IQSEC2.

More Related Videos

Evaluation of Synaptic Multiplicity Using Whole-cell Patch-clamp Electrophysiology
10:52

Evaluation of Synaptic Multiplicity Using Whole-cell Patch-clamp Electrophysiology

Published on: April 23, 2019

13.6K
Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
08:06

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient

Published on: September 3, 2014

31.9K

Related Experiment Videos

Last Updated: Jan 14, 2026

Electroconvulsive Seizures in Rats and Fractionation of Their Hippocampi to Examine Seizure-induced Changes in Postsynaptic Density Proteins
09:07

Electroconvulsive Seizures in Rats and Fractionation of Their Hippocampi to Examine Seizure-induced Changes in Postsynaptic Density Proteins

Published on: August 15, 2017

12.6K
Evaluation of Synaptic Multiplicity Using Whole-cell Patch-clamp Electrophysiology
10:52

Evaluation of Synaptic Multiplicity Using Whole-cell Patch-clamp Electrophysiology

Published on: April 23, 2019

13.6K
Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
08:06

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient

Published on: September 3, 2014

31.9K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • IQSEC2 is crucial for neuronal development and synaptic plasticity.
  • IQSEC2 regulates synaptic signaling through Ca2+-dependent mechanisms.

Purpose of the Study:

  • To investigate the role of IQSEC2 in postsynaptic density assembly and dynamics.
  • To elucidate the mechanism of IQSEC2-mediated synaptic regulation.

Main Methods:

  • In vivo mouse models
  • In vitro biochemistry
  • Analysis of synaptic transmission and plasticity in hippocampal neurons

Main Results:

  • IQSEC2 orchestrates postsynaptic density assembly via Ca2+-triggered phase separation.
  • A specific mutation (F367A) in IQSEC2 leads to constitutive activity, elevated synaptic transmission, and impaired plasticity.
  • Deficits in spatial learning were observed in mice with the Iqsec2_F367A mutation.

Conclusions:

  • IQSEC2 bidirectionally modulates synaptic strength through Ca2+-dependent phase separation.
  • Disruption of IQSEC2 phase separation is implicated in IQSEC2-related neurodevelopmental disorders.