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Gap Junctions

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...

Gap Junctions

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...

G Protein-coupled Receptors

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...

G-protein Coupled Receptors

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.

G-protein Coupled Receptors

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.

Contact-dependent Signaling

Contact-dependent Signaling

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...

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Related Experiment Video

Updated: Jun 1, 2026

RNA Isolation from Mouse Ocular Lens Epithelium and Fiber Cell Bulk Masses

RNA Isolation from Mouse Ocular Lens Epithelium and Fiber Cell Bulk Masses

Published on: October 10, 2025

PKCγ, role in lens differentiation and gap junction coupling.

Satyabrata Das¹, Huan Wang, Samuel A Molina

¹Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA.

Current Eye Research

|May 24, 2011

Summary

Protein kinase C gamma (PKCγ) significantly regulates gap junction coupling in the eye lens. Its absence in knockout mice increases Cx43 expression and enhances cell-to-cell communication in lens fibers.

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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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Published on: January 12, 2012

Area of Science:

Ophthalmology
Cell Biology
Physiology

Background:

Gap junction coupling is crucial for lens transparency and function.
Protein kinase C gamma (PKCγ) is a potential regulator of lens gap junctions.

Purpose of the Study:

To investigate the role of PKCγ in regulating gap junction coupling within the normal lens.
To compare gap junction properties in wild type (WT) and PKC-γ knockout (KO) mouse lenses.

Main Methods:

Utilized Western blotting, confocal microscopy, immunoprecipitation, and RT-PCR to assess gap junction protein and message expression.
Measured gap junction coupling conductance and pH gating in intact lenses via impedance studies.

Main Results:

No significant differences in lens size, clarity, or Cx46/Cx50 expression between WT and KO mice.
PKCγ knockout lenses showed a ~150% increase in total Cx43 protein expression, with Cx43 extending into fiber cells.
Gap junction coupling conductance increased by 34% in differentiating fibers and 82% in mature fibers of KO lenses compared to WT.

Conclusions:

PKCγ plays a critical role in regulating gap junction expression and coupling in the normal lens.
The absence of PKCγ leads to altered Cx43 distribution and significantly enhanced gap junction communication in the lens.