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Related Concept Videos

Gap Junctions01:37

Gap Junctions

55.5K
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...
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Gap Junctions01:27

Gap Junctions

8.7K
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...
8.7K
Contact-dependent Signaling01:19

Contact-dependent Signaling

45.5K
Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
Gap Junctions
In animal cells, gap junctions are formed...
45.5K
Tight Junctions01:29

Tight Junctions

6.1K
Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
6.1K
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

8.2K
The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
8.2K
Overview of Cell-Cell Junctions01:14

Overview of Cell-Cell Junctions

27.6K
The complex three-dimensional arrangement of cells in any multicellular organism is defined and maintained by interactions of cells with each other and the extracellular matrix. Cell-cell junctions are specialized structures where the multi-protein complexes on one cell interact with the multi-protein complexes on another  cell. These cell junctions are classified  into three main types based on their function — occluding, anchoring, and gap junctions.
Occluding or Tight...
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Related Experiment Video

Updated: Nov 3, 2025

Cut-loading: A Useful Tool for Examining the Extent of Gap Junction Tracer Coupling Between Retinal Neurons
10:11

Cut-loading: A Useful Tool for Examining the Extent of Gap Junction Tracer Coupling Between Retinal Neurons

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PTEN Expression Regulates Gap Junction Connectivity in the Retina.

Ashley M Chen1, Shaghauyegh S Azar1, Alexander Harris1

  • 1Department of Neurobiology, David Geffen School of Medicine at Los Angeles, University of California, Los Angeles, Los Angeles, CA, United States.

Frontiers in Neuroanatomy
|June 7, 2021
PubMed
Summary

Deleting one copy of the phosphatase and tensin homolog (PTEN) gene in retinal ganglion cells altered their electrical connections. This impacts visual processing and may limit PTEN pathway therapies for vision loss.

Keywords:
PTEN (phosphatase and tensin homolog deleted on chromosome 10)connexin (Cx36)degenerationgap junction (connexin)retinaretinal ganglion cells

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Recording Gap Junction Current from Xenopus Oocytes
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Cut-loading: A Useful Tool for Examining the Extent of Gap Junction Tracer Coupling Between Retinal Neurons
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Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells
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Recording Gap Junction Current from Xenopus Oocytes
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Area of Science:

  • Neuroscience
  • Ophthalmology
  • Genetics

Background:

  • The phosphatase and tensin homolog (PTEN) pathway is a target for treating retinal diseases and vision loss.
  • Retinal ganglion cells (RGCs) are crucial for visual information processing and are vulnerable in various neurological conditions.

Purpose of the Study:

  • To investigate the impact of deleting one copy of the Pten gene on α-ganglion cells in the mouse retina.
  • To understand how Pten haploinsufficiency affects RGC structure, connectivity, and potential therapeutic strategies.

Main Methods:

  • Utilized a mouse model with one Pten gene copy deleted (Pten+/-).
  • Examined dendritic structure and gap junction coupling in α-ganglion cells.
  • Quantified connexin36 puncta, essential for electrical synapses.

Main Results:

  • Pten+/- α-ganglion cells showed minor dendritic changes but significant reductions in gap junction coupling.
  • A notable increase in novel coupling between OFF α-ganglion cells and displaced amacrine cells was observed.
  • Connexin36 puncta decreased by over 50% in OFF α-ganglion cells, indicating impaired electrical synapse function.

Conclusions:

  • Reduced and aberrant gap junction connectivity in Pten+/- α-ganglion cells disrupts normal visual processing.
  • These connectivity anomalies may hinder the efficacy of therapies targeting the PTEN pathway for retinal degeneration and related neurological diseases.