Cell junction

In vertebrates, there are three major types of cell junction: • Adherens junctions, desmosomes and hemidesmosomes (anchoring junctions) • Gap junctions (communicating junction) • Tight junctions (occluding junctions) Invertebrates have several other types of specific junctions, for example septate junctions (a type of occluding junction) Three types of anchoring junctions are observed, and differ from one another in the cytoskeletal protein anchor as well as the transmembrane linker protein that extends through the membrane: Anchoring-type junctions not only hold cells together but provide tissues with structural cohesion. These junctions are most abundant in tissues that are subject to constant mechanical stress such as skin and heart. Hemidesmosomes Hemidesmosomes form rivet-like links between cytoskeleton and extracellular matrix components such as the basal laminae that underlie epithelia. Like desmosomes, they tie to intermediate filaments in the cytoplasm, but in contrast to desmosomes, their transmembrane anchors are integrins rather than cadherins. Adherens junctions Adherens junctions share the characteristic of anchoring cells through their cytoplasmic actin filaments. Similarly to desmosomes and hemidesmosomes, their transmembrane anchors are composed of cadherins in those that anchor to other cells and integrins (focal adhesion) in those that anchor to extracellular matrix. There is considerable morphological diversity among adherens junctions. Those that tie cells to one another are seen as isolated streaks or spots, or as bands that completely encircle the cell (adhesion belts). The band-type of adherens junctions is associated with bundles of actin filaments that also encircle the cell just below the plasma membrane. Spot-like adherens junctions called focal adhesions help cells adhere to extracellular matrix. The cytoskeletal actin filaments that tie into adherens junctions are contractile proteins and in addition to providing an anchoring function, adherens junctions are thought to participate in folding and bending of epithelial cell sheets. Thinking of the bands of actin filaments as being similar to 'drawstrings' shows how contraction of the bands within a group of cells would distort the sheet into interesting patterns. This is possible due to six connexin proteins interacting to form a cylinder with a pore in the centre called a connexon. The connexon complexes stretches across the cell membrane and when two adjacent cell connexons interact, they form a complete gap junction channel. including their role in the uniform contractile of the heart muscle. Retinal and skin cells are also dependent on gap junctions in cell differentiation and proliferation. Tricellular junctions are also implicated in the regulation of cytoskeletal organization and cell divisions. In particular they ensure that cells divide according to the Hertwig rule. In some Drosophila epithelia, during cell divisions tricellular junctions establish physical contact with spindle apparatus through astral microtubules. Tricellular junctions exert a pulling force on the spindle apparatus and serve as a geometrical clue to determine orientation of cell divisions. ==Cell junction molecules==

The molecules responsible for creating cell junctions include various cell adhesion molecules. There are four main types: selectins, cadherins, integrins, and the immunoglobulin superfamily. Selectins are cell adhesion molecules that play an important role in the initiation of inflammatory processes. The functional capacity of selectin is limited to leukocyte collaborations with vascular endothelium. There are three types of selectins found in humans; L-selectin, P-selectin and E-selectin. L-selectin deals with lymphocytes, monocytes and neutrophils, P-selectin deals with platelets and endothelium and E-selectin deals only with endothelium. They have extracellular regions made up of an amino-terminal lectin domain, attached to a carbohydrate ligand, growth factor-like domain, and short repeat units (numbered circles) that match the complementary binding protein domains. Cadherins are calcium-dependent adhesion molecules. Cadherins are extremely important in the process of morphogenesis – fetal development. Together with an alpha-beta catenin complex, the cadherin can bind to the microfilaments of the cytoskeleton of the cell. This allows for homophilic cell–cell adhesion. The β-catenin–α-catenin linked complex at the adherens junctions allows for the formation of a dynamic link to the actin cytoskeleton. Integrins act as adhesion receptors, transporting signals across the plasma membrane in multiple directions. These molecules are an invaluable part of cellular communication, as a single ligand can be used for many integrins. Unfortunately, these molecules still have a long way to go in the ways of research. Immunoglobulin superfamily are a group of calcium independent proteins capable of homophilic and heterophilic adhesion. Homophilic adhesion involves the immunoglobulin-like domains on the cell surface binding to the immunoglobulin-like domains on an opposing cell's surface while heterophilic adhesion refers to the binding of the immunoglobulin-like domains to integrins and carbohydrates instead. Cell adhesion is a vital component of the body. Loss of this adhesion effects cell structure, cellular functioning and communication with other cells and the extracellular matrix and can lead to severe health issues and diseases. ==References==