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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...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

Catenins

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...

Tension Response at Adherens Junctions

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...

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: May 21, 2026

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells

Published on: July 16, 2013

Posttranslational modifications in connexins and pannexins.

Scott R Johnstone¹, Marie Billaud, Alexander W Lohman

¹Robert M. Berne Cardiovascular Research Center, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.

The Journal of Membrane Biology

|June 29, 2012

Summary

Posttranslational modifications like ubiquitination and glycosylation are crucial for regulating connexin and pannexin proteins. These modifications ensure proper protein function and cellular processes.

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Area of Science:

Cellular Biology
Molecular Biology
Biochemistry

Background:

Posttranslational modifications are essential for protein function and cellular regulation.
These modifications involve adding chemical groups like phosphates or sugars to amino acids.
Connexins and pannexins are key proteins involved in cellular communication.

Purpose of the Study:

To review the evidence for various posttranslational modifications in connexin and pannexin proteins.
To understand the regulatory role of these modifications in protein function.
To consolidate current knowledge on connexin and pannexin posttranslational modification.

Main Methods:

Literature review of scientific publications.
Analysis of studies reporting on connexin and pannexin modifications.
Synthesis of evidence for ubiquitination, glycosylation, phosphorylation, and S-nitrosylation.

Main Results:

Evidence supports the occurrence of ubiquitination, glycosylation, phosphorylation, and S-nitrosylation in connexins and pannexins.
These modifications significantly impact the function and regulation of these protein families.
A variety of posttranslational modifications are implicated in connexin and pannexin biology.

Conclusions:

Posttranslational modifications are integral to the regulation of connexin and pannexin proteins.
Understanding these modifications is key to deciphering protein function and cellular signaling.
Further research into specific modification types and their functional consequences is warranted.