2011 Group 5 Project

From CellBiology

Adherens Junctions

Residual membrane tethers in disrupted Adherens Junctions


Epithelial sheet is joined by the epithelial cells; joining together by various types of junctions, in order to coordinate the tissue. Adhedrens junction is one of the many junctions that contribute to this cell-to-cell joint [1]. This junction occurs mainly near to the apical surface of cell after the tight junction. The adherens junction is formed mainly by the E-cadherin protein; a type of integral membrane protein, that binds to identical E-cadherin protein of adjacent cell[2]. This homophilic binding leads to the binding of the actin filament within the epithelial cells. Through this adherens junction, the adhesion belt is formed through out the epithelial sheet and with the actin filament contracting within the cell, the shape of epithelial sheet changes. As the apical surface of the sheet shrinks to the position of adherens junction, the sheet can be rolled up in different levels and this can be a very important factor in the development of neural tube and eye lens in embryonic development.[3]


1839- Theodor Schwann and Matthias Schleiden hypothesis that “animal cells might fuse at specific points via cytoplasmic bridges”.[4]

1961- Farquhar and Palade define three of the four cell to cell junction , one of them being adherens junctions. Their location below tight junctions is also identified.[5]

1977– Cadherins, the adhesion molecule are first identified in adherens junctions by Masatoshi Takeichi.[6]

1982- “N-cadherin was first identified in 1982 (Grunwald et al., 1982) as a 130 kD molecule in the chick neural retina that was protected by calcium from proteolysis”.[7]

Shoichiro Tsukita

1989- Tsukita and Tsukita are the first to isolate intact adherens junctions from preparation of rat liver hepatocytes.[8]

1992- Tsukita et al suggest that alpha catenin links the cadherin complex to the cytoskeleton.[9]

2000- “N-cadherin can engage also in heterotypic homophilic and heterophilic interactions with other caherins (Shan et al, 2000)”[10]


Adherens Junction Diagram.jpg

Adherens junctions are cell to cell junctions that connect bundles of actin filaments between cells. These specialized junctions are formed from proteins called cadherins.[2] Cadherins are cell adhesion molecules that mediate calcium dependent junctions.

Homophillic binding of cadherin dimers

There are classical and non-classical types of cadherin protein molecules, together making up what is called the cadherin superfamily of proteins. Classical cadherins including E-cadherin, N-cadherin and P-cadherin are associated with adherens junctions whereas non-classical cadherins including Desmocollin and Desmoglein are associated with desmosomes. Studies have shown that cadherin binding is strictly homophilic binding, meaning only two of the same types of cadherin protein molecules may bind together. This was proved by mixing cells expressing different cadherin types, resulting in segregation based on their types. An interesting example of this occurs during neural tube formation during embryo development. The separation of the ectoderm layer from the forming neural tube can be attributed to the expressions of two different cadherins, E- and N-cadherin in the separate layers, meaning these two tissues form independent of each other. [11]

Linked cadherin molecules

Cadherins are glycoprotein chains approximately 700-750 amino acid units long which are folded into polypeptide chain repeats. These repeats are alternated with calcium ions which function to hold the chain together into a stiff structure, strong enough to link with other cadherin molecules in adjacent cells forming a strong cell adhesion junction.[2]This means adherens junctions depend on extracellular calcium to function properly in cell adhesion.

The transmembrane cadherin protein molecules are connected to intracellular actin filaments in cells via anchor proteins alpha and beta catenin.

Epithelial sheet stained for beta catenin at cell junctions

These extra linker proteins are key in the structure of adherens junctions as cadherin molecules are not strong enough to bind the actin cytoskeletons of two cells by themselves.[12]

An adhesion junction cannot be formed without the formation of a cadherin and beta catenin complex as the first step. The 781 amino acid beta catenin binds strongly to the cadherin by a process of phosphorylation and it has been shown that mutations at these phosphorylation sites on the proteins can effectively reduce cell adhesion.[13] It was originally thought that alpha catenin acted as the bridge holding the cadherin-beta catenin complex to the actin filaments. Further research has suggested that alpha catenin doesn't join these proteins together but actually acts as a regulatory protein, regulating filamentous actin dynamics.[14] Alpha catenin molecules function to bundle actin fibers into stronger filaments to support the junction stability.[15]

VIDEO:Adherens junction structure animation | This three dimensional animated video shows how two cells with like cadherin molecules bind together, gathering more cells forming a stable epithelial sheet. It also depicts a key function of these junctions detailed below of the separation of the neural tube from the ectodermal layer during embryo development.


Adherens junctions have a variety of functions, they particularly play a vital role in cell to cell adhesion and cell to matrix adhesion. Furthermore adherens junctions are or have been hypothesised to be important factors in the proper function of tissue homeostasis, permeability, cell signalling, transportation, embryogenesis and neural tube formation. So far there is knowledge that adherence junctions play a vital role in many biological processes and what the outcomes would be if there is a dysfunction with this adhesion type, such as gene deletion or mutation. However the exact molecular mechanism in which this junctions functions is still an area of uncertainty.

The ability of adherens junction to maintain cell to cell adhesion allows for the maintenance of the epithelial barrier, which acts to protect us from the outside world, as well as preventing unnecessary water loss. An excellent example the crucial roles adherens junctions play in epithelial adhesion is the experiment where the alpha-catenin is specifically deleted in mice. The results of this study showed detachment of the epidermis, associated with the loss of intercellular adhesion and adherens junctions [16].

Adherens Junctions in epithelial cells

Adherens junction have role in the connectivity of endothelial cells and the homeostasis of the blood vessels by “controlling the movement of solutes between the blood stream and the sourrounding tissue”[17] and the infiltration of leucocytes between blood and tissue in particular at sites of inflammation. One of the theories on the molecular basis, on the maintenance of vascular permeability and homeostasis is that the actomyosin that is anchored to the adherens junctions contract to allow for opening up of the adherens junction.[18].

Furthermore adherens junction have been seen playing a vital role in embryogenesis as they regulate epidermal assembly and cell polarity. During embryogenesis if catenin molecules are absent or mutated, the embryoblast will lose its adhesion and fail to continue its development[19] In addition the N-cadherin molecules function in the development of an embryo were it is regulated as necessary for the migration of neural crest cells and the closure of the neural tube.[20]

Importance and Regulation

Remodeling of Adherens Junctions

The Adherens Junction is an essential feature in mammals; it provides the protection to our skin (epidermis). On top of that the ability to contract the epithelial or endothelial tissue make this junction is an important factor when it comes to embryonic development [3]. It gives rise to the structure of neural tube and lens of the eye. The Adherns Junction also regulate the vescular permeability. The impaired function can lead to several pathological conditions which can lead to fatal dysfuction such as, inflammation, sepsis, ischemia and diabetes. The ischemic tissue injury can also cause different sorts of diseases such as stroke or myocardial infarction. [21]

Adherens Junction.JPG

The important feature in Adhrens junction is the Ca2+ dependent Cadherin intermembrane protein, the catenin cytoplasm protein and the actin filaments. The regulation of this Junction can be at the level of intercellular or extracellular level. The regulation can occur at the site of the E-cadherin protein complex formation, the level of cadherin/catenin (which binds to actin filament) binding site or the cadherin/cadherin homophilic binding site.

Concentration of Ca2+ is important in the extracellular space. The calcium binds the Cadhedrin proteins together in order for the Adhesion Junction to be formed. With out this the cell-cell homophilic binding of adhesion cells are not possible. Therefore the level of Ca2+ can be a good regulator for the Adherens Junction. The ranges of extra cellular signals that can regulate the Adherens Junction at this site are; growth factors, the peptide hormones and …etc. [22].

The Rho family of GTPase are another essential regulator for the Junction. This occurs at the site of cytoplasm tail of E-cadherin interacting with the actin cytoskeleton via catenin which binds the actin and cadhedrin together. The Rho family act as the the ‘molecular switch’ which allows the cycle inbetween GTP-bound stace and GDP-bound state, allowing regulation of both the assembly and disassembly of adherens junction by gathering of E-cadherin, b-catenin and actin at the site of cell-cell contacts. [23] Rho Family GTPases and Cellular Transformation

743px-Protein IQGAP1 PDB 1x0h.png

Also the IQGAP1 seem to be a important regulator co-working with Rho family GTPases, to regulate cell adhesion, polarization and migration. When it is over expressed, it interacts with β-catenin which dissociate of α-catenin from the cadherin-catenin complex, hense reducing the E-cadherin based cell-cell adhesion. Vice versa, the activated Rac1 and Cdc42 positively regulate E-cadherin-mediated cell-cell adhesion by inhibiting the interaction of IQGAP1 with β- catenin [24]. It not only down regulate at Adherens Junction but lead to estabilishment of polarised cell morphology and directional cell migration.

There are more factors that regulate the Adherens junctions. However, there are more areas to be researched. The importance of this junction if quite clear and if this can be controlled correctly, it can be a huge step in medical fields.

Abnormalities of Adherens Junctions

Listeria monocytogenes

Listeria monocytogenes - Meningitis, Encephalitis, Septicemia, Endocarditis, Abortion, Abscesses, Listeriosis

Listeria monocytogenes, an intracellular bacterium, is the causative agent of listeriosis. It is one of the most virulent foodborne pathogens, with 20 to 30 percent of clinical infections resulting in death. It Causes invasive disease by crossing the intestinal epithelial barrier. This process depends on the interaction between the bacterial surface protein Internalin A and the host protein E-cadherin. Biochemical studies have shown that both tight junction proteins and adherens junction proteins are degraded in apoptotic cells, which may facilitate their detachment from neighboring cells. By detaching, these junctions are no longer able to function and encounter apoptosis. [25]

Polycystic Kidney Disease

Polycystic kidney disease is a disease of the nephron, characterised by the formation of multiple renal tubular cysts, leading to endstage renal failure. Autosomal Dominant Polycystic Kidney Disease is caused by mutations in the genes encoding polycystin-1 and/or polycystin-2, but results in epithelial cells with disrupted adherens junctions and compromised beta-catenin signaling pathways. More information can be found Autosomal dominant polycystic kidney disease: the last 3 yearsAutosomal dominant PKD

Ulcerative Colitis and colorectal carcinomas

Ulcerative Colitis

CD97 is a protein that in humans is encoded by the CD97 gene and induces specific signaling that results in a decrease of proteolytic digestion of β-catenin. It is a major factor in stabilisation within adherens junctions and thus causes breakdowns within the structure of the junction itself. [26] This occurs in both Ulcerative Colitis and Colorectal carcinomas as both are located in the colon. [27]

Dengue Fever

Increased vascular permeability is a main feature in severe dengue virus infections as well as the dysfunction of endothelial cells to contributing to the pathogenesis of dengue hemorrhagic fever/dengue shock syndrome. Small signaling GPTase enzymes (that regulate intracellular Actin dynamics) are significant elements of endothelial barrier function regulation and has been implicated in the regulation of actin remodeling and intercellular junction formation. In the absence of vasoactive stimuli, dominant negative Rac1 (a dominant enzyme in this GTPase family) increases endothelial permeability and affects adherens and tight junctions. [28]

Transmission electron micrograph of hantavirus


Recent disease research by Gorbunova E., Gavrilovskaya I. and Mackow, R has shown that the Anders and Hantaan Viruses (pathogenic hanatviruses) disrupt fluid barrier properties of endothelial cell adherens junctions by enhancing the specific cadherin pathway responses which increase paracellular permeability. For more information please follow the link... Pathogenic Hantaviruses Andes Virus and Hantaan Virus Induce Adherens Junction Disassembly by Directing Vascular Endothelial Cadherin Internalization in Human Endothelial Cells

Current Research

Placenta Growth Factor-1 Exerts Time-Dependent Stabilization of Adherens Junctions Following VEGF-Induced Vascular Permeability 2011

Cai et al. discuss the role of the placenta growth factor (PIGF) and its isoforms 1 and 2 in regulating vascular permeability associated with the rapid localisation of specific cadherin to the plasma membrane, specifically in adherens Junctions. The time period in which this growth factor exerts its effect on the stability of the junction highlights its ability to be used as an endogenous anti-permibility factor whose effectiveness is limited to a precise time point following vascular injury. [29]

FPEX Research by the Idaho National Laboratory

Adherens junctions connect stress fibres between adjacent endothelial cells 2010

Endothelial cell-cell junctions can attach to the ends of stress fibres instead of to cortical F-actin, forming structures that are named discontinuous adherens junctions. These junctions are highly dynamic and are increased in response to tumour necrosis factor (TNF)-α, correlating with the appearance of stress fibres. Theses fibres from neighbouring cells are physically connected through discontinuous Adherens Junctions, and that stress fibres can be stabilized by Adherens Junction-associated multi-protein complexes distinct from focal adhesions.[30]

PLEKHA7 Is an Adherens Junction Protein with a Tissue Distribution and Subcellular Localization Distinct from ZO-1 and E-Cadherins 2010

The pleckstrin-homology-domain-containing protein PLEKHA7 was recently identified by Pulimeno et al. as a protein linking the E-cadherin- complex to the microtubule cytoskeleton. They were able to characterise. The proteins function, expression and localisation whist also labelling the junctions regions within cultured kidney cells. Specifically they established that definitively establishes that PLEKHA7 is localized at the adherens junctions in colonic epithelial cells.[31]

Overexpression of CD97 in Intestinal Epithelial Cells of Transgenic Mice Attenuates Colitis by Strengthening Adherens Junctions 2010

The adhesion G-protein-coupled receptor CD97 is present in normal colonic enterocytes but overexpressed in colorectal carcinoma. Noticing this, Becker et al. researched showed that this CD97 antigen increases the structural integrity of enterocytic adherens junctions by increasing and stabilizing junctional β-catenin, and as such, the heavily cadherin dependent Adherens junctions. Thereby, this paper explains how CD97 regulates intestinal epithelial strength and attenuating experimental colitis.[32]

A Cell Motility Screen Reveals Role for MARCKS-Related Protein in Adherens Junction Formation and Tumorigenesis 2009

Invasion through the extracellular matrix is important for wound healing, immunological responses and metastasis.Through use of Invasion-based motility assays, Finlayson et al were able to identify an antisnese related protein whose family member (MPR) was involved in tumor growth, invasion and metastesis in multiple human cancers. They were also able to identify an increased in the number of E-cadherin, β-catenin and adenomatous polyposis coli (APC) protein at sites of cell-cell contact in cells with MRP knockdown suggesting formation of adherens junctions. As a whole their data suggest that reducing MRP expression promotes formation of adherens junctions, allowing collective cell migration, but interferes with oncogenic β-catenin signaling and tumorigenesis.[33]

Microscopy by the Idaho National Laboratory

Other types of Cell Junctions

Types of Cell Junctions
Junction Type of junction Key Proteins Function Diagram
Tight Junction OCCLUDING junction: Seals cells together to prevent leakage of molecules between them and through the epithelial sheet.[34] Claudins and occludins[3] Tight junctions are the junctions between cells that form an epithelial sheet throughout the body. They seal the adjacent cells together in a band just below the apical surface, the surface that is exposed to the lumen. They are important in preventing molecules leaking between the cells, providing control of passage of materials through the epithelial sheet as the cells must diffuse through the cells themselves to pass through.[35] Tight junction.png
Gap Junction COMMUNICATING junction: Mediates the passage of chemical or electrical signals between cells.[34] Connexons[3] Gap junctions form channels between cells approximately 1.5-2 nanometers in diameter for the passage of ions and small molecules. These function to regulate the membrane potential between cells and allow electrical impulses to pass between cells. Examples of this includes electrical impulses passing between cardiac muscle cells creating the heart beat. Also gap junctions provide the contractions of the smooth muscle cells of the uterus during birth.[36][37] Gap junction cartoon1.jpg
Desmosomes ANCHORING junction: mechanically attaches cells to their neighbors.[34] Cadherins [3] These function to attach two epithelial cells together by their intermediate filaments, in particular holding the stratified epithelium of the epidermis together. These are similar to adherens junctions as they anchor two cells together by cadherin proteins which bind in a strong homophilic way.[38] Desmosome image.png
Tunneling Nanotubes COMMUNICATING junction: Mediates the passage of chemical or electrical signals between cells over a longer distance.[39] Motor protein myosin Va[40] Tunneling nanotubes form thin membrane channels between cells over a longer distance than gap junctions, up to several cell diameters in distance[41], and are also wider in diameter, approximately 50-200 nanometers wide.[42] They not only allow the passage of proteins between cells but also of organelles. Due to their sensitive structure they have only recently been discovered and studies on them have been limited. Nanotube.jpg
Hemidesmosome ANCHORING junction: Mechanically attaches cells to its basal lamina.[34] Integrin proteins[3] With the appearance of half a desmosome, hemidesmosomes anchor cells to the basal lamina. Even though they have a similar appearance, hemidesmosomes bind using integrin proteins and not the cadherins that desmosomes use. They play important roles in the basal cells of stratified epithelia, but particularly in epidermal to dermal adhesion of the skin. Integrin proteins in the basal plasma membrane of the epithelial cells bind to laminin, an extracellular matrix protein in the basal lamina.[3] Tracheal hemidesmosomes.JPEG
Neuromuscular Junction COMMUNICATING junction: Mediates the passage of chemical or electrical signals between cells. Acetylcholine receptor[43] associated with rapsyn[44] and cortactin proteins[45] A neuromuscular junction is the synapse of the axon terminal of a motor neuron with the end plate of a muscle fibre. The signal transmission from the the neuron to the muscle cell occurs due to the release of the chemical acetylcholine which binds to a protein receiver on the muscle called the acetylcholine receptor. Neuromuscular junctions are essential for muscle function in vertebrates.[46]
Detailed view of a neuromuscular junction:
1. Presynaptic terminal
2. Sarcolemma
3. Synaptic vesicle
4. Nicotinic acetylcholine receptor
5. Mitochondrion

External Links

Myofibroblast Adherens Junctions Image



Actin Cytoskeletal 43 kD protein forming the backbone of the cytoplasmic microfilament system and the thin filament system of muscle sacomeres. In humans, there are distinct muscle (4 alpha-skeletal, alpha-cardiac, alpha-smooth, gamma-smooth) and non-muscle (2 cytoskeletal beta-, gamma-) actin isoforms. Exists as globular actin monomer (G-actin) and microfilament polymer (F-actin).

Adenomatous Polyposis Coli Protein A negative regulator of beta-catenin signaling. These gene is associated with familial adenomatous polyposis (FAP), an inherited disorder characterized by the development of myriad polyps in the colon. The gene is located on chromosome 5. [47]

Amino acid One of the 20 building blocks of protein. The sequence of amino acids in a protein and, hence, the function of that protein are determined by the genetic code in the DNA. Amino acids are molecules that (in technical terms) contain a basic amino (NH2) group, an acidic carboxyl (COOH) group and a side chain attached to an alpha carbon atom. [48]

Antisnese Having a sequence of nucleotides complementary to a coding sequence, which may be either that of the strand of a DNA double helix that undergoes transcription, or that of a messenger RNA molecule. [49]


Cadherins Calcium-dependent cell-adhesion molecules.[50]

Catenin Any of a family of 80-102-kilodalton proteins that are thought to have a major role in regulation of cell-to-cell adhesion, which is related to their interaction with E-cadherin and the actin cytoskeleton.

CD97 Primary antibodies; Rabbit polyclonal to CD97 Immunogen: A portion of amino acids 220-270 of human CD97

Cytoskeleton Set of 3 filament systems intermediate filaments, actin filaments, and microtubules. Eukaryotic cells have a cytoplasmic and a nuclear cytoskeleton with different organisations and filaments.


Enterocytes A cell that lines the intestinal wall.


F-actin Actin is a globular, roughly 42-kDa protein found in all eukaryotic cells (the only known exception being nematode sperm) where it may be present at concentrations of over 100 μM.


Glycoprotein A molecule that consists of a carbohydrate plus a protein.[51]


Hantavirus A type of virus carried by rodents causing severe respiratory infections in humans and, in some cases, hemorrhaging, kidney disease, and death.

homophilic binding


Ulcerative Colitis a serious chronic inflammatory disease of the large intestine and rectum characterized by recurrent episodes of abdominal pain and fever and chills and profuse diarrhea.


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Coordinator Comment to all Groups

I will add a general comment that will be the same to all groups under this heading.

Referencing Extension Problem

--Mark Hill 13:16, 3 May 2011 (EST) As mentioned in the lecture, I am aware of the referencing extension problem on your project pages. I have the following temporary solution, of removing the extension, so that groups can continue to add content to their project pages. I am also giving everyone a 1 week extension before the peer assessment.

This should only be done if your project page is not allowing you to save changes!

A. The Easy Way....

The following 4 steps can be done on the webpage or select all content in edit mode, copy and paste into a text editor. All steps must be completed before you attempt to save.

  1. In page edit mode, find all <pubmed> reference tags.
  2. Replace this tag with [http://www.ncbi.nlm.nih.gov/pubmed/ Note, there should be no spaces between the internet address and the pmid number.
  3. Now find all </pubmed> reference tags.
  4. Replace this second tag with ]

This will generate a numbered reference list that we can later fix up.

B. The Better Looking Result....

Whatever is between the <ref> </ref></pubmed> tags is what will appear in your reference list, so you can format the reference and link to appear in your reference list.

2011 Projects: Synaptic Junctions | Gap Junctions | Tight Junctions | Desmosomes | Adherens Junctions | Neuromuscular Junction