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Related Concept Videos

Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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...
Gap Junctions01:27

Gap Junctions

The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
Gap Junctions01:37

Gap Junctions

Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
Electrical Synapses01:28

Electrical Synapses

Electrical synapses found in all nervous systems play important and unique roles. In these synapses, the presynaptic and postsynaptic membranes are very close together (3.5 nm) and are actually physically connected by channel proteins forming gap junctions.
Gap junctions allow the current to pass directly from one cell to the next. In contrast, in the chemical synapse, the neurotransmitters carry the information through the synaptic cleft from one neuron to the next. They consist of two...

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Related Experiment Video

Updated: Jun 12, 2026

Inhibitory Synapse Formation in a Co-culture Model Incorporating GABAergic Medium Spiny Neurons and HEK293 Cells Stably Expressing GABAA Receptors
07:51

Inhibitory Synapse Formation in a Co-culture Model Incorporating GABAergic Medium Spiny Neurons and HEK293 Cells Stably Expressing GABAA Receptors

Published on: November 14, 2014

Organization of synaptic junction proteins.

A P Smith1, H H Loh

  • 1Department of Pharmacology, University of California, San Francisco, San Francisco, CA 94137, U.S.A.

Neurochemistry International
|May 22, 2010
PubMed
Summary
This summary is machine-generated.

Brain synaptic junctions utilize disulfide bonds for polypeptide cross-linking, with non-covalent interactions inaccessible to surface treatments. This suggests a model for forming stabilized junctional membranes from fluid extra-junctional membranes during synaptogenesis.

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Related Experiment Videos

Last Updated: Jun 12, 2026

Inhibitory Synapse Formation in a Co-culture Model Incorporating GABAergic Medium Spiny Neurons and HEK293 Cells Stably Expressing GABAA Receptors
07:51

Inhibitory Synapse Formation in a Co-culture Model Incorporating GABAergic Medium Spiny Neurons and HEK293 Cells Stably Expressing GABAA Receptors

Published on: November 14, 2014

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture
10:17

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Published on: August 2, 2019

An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins
09:33

An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins

Published on: June 26, 2018

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Synaptic junctions are crucial for neuronal communication.
  • The structural integrity of synaptic junctions relies on protein-protein interactions.
  • Understanding these interactions is key to deciphering synapse formation and function.

Purpose of the Study:

  • To investigate the nature of polypeptide interactions within brain synaptic junctions.
  • To determine the role of disulfide bonds and non-covalent interactions in maintaining junctional structure.
  • To explore the relationship between extra-junctional and junctional membrane composition.

Main Methods:

  • Isolation of brain synaptic junction preparations.
  • Treatment with reducing agents (e.g., ?-mercaptoethanol) and various non-covalent bond disrupting reagents.
  • Analysis of polypeptide cross-linking and association with membrane fractions under different solvent conditions (e.g., NaOH, Triton X-100).

Main Results:

  • Most synaptic junction polypeptides are cross-linked by disulfide bonds, which reform after reduction.
  • Non-covalent interactions are not disrupted by common reagents, suggesting they are internal or shielded.
  • Synaptic junction proteins remain associated with reduced membranes in harsh solvents that extract proteins from extra-junctional membranes.
  • Extra-junctional membrane polypeptides can form disulfide cross-links under specific conditions.

Conclusions:

  • Disulfide bonds play a primary role in stabilizing synaptic junction structure.
  • Non-covalent interactions are likely located within the lipid bilayer or at specific contact points.
  • A model is proposed where fluid extra-junctional membrane transforms into stabilized junctional membrane via disulfide cross-linking during synaptogenesis.