Intercellular Communication and Gap Junction

The gap junction has six subunits of the connexin protein. These subunits are arranged as the annular torus hexamer structure. This structure is arranged around the aqueous pore, which is referred to as the connexon or the hemichannel. Connexon is composed of two types of channels as homomeric and heteromeric. The homomeric is made of a single protein of connexin, whereas, the heteromeric is made of more than two different proteins of connexin. These connexons are then arranged on the cell membrane and attached with the other connexon of the adjacent cell, forming a gap junction. Hence, this intracellular channel is referred to as the gap junction channel. the gap junction channel can of various types depending on the arrangement of homomeric and heteromeric between the adjacent cell membranes. When all the connexon of gap junction is formed by the same protein composition, they are considered as the homotypic channels. Whereas, if all the connexion of gap junction is composed of different protein composition then are considered as the heterotypic channels. The main function of the gap junction is the transportation of small molecules like ions, ADP, ATP, cAMP, small peptides, inositol triphosphate, amino acids, oligonucleotides, glucose, and cyclic nucleotides.

Connexin is a protein that consists of four alpha-helix on transmembrane. They are named TM1, TM2, TM3, and TM4. They are connected with the intracellularly present single loop and other extracellularly found two loops. They have shorter N-terminal and longer C-terminal, which are eventually facing the cytoplasm of the cell membrane. The extracellular two-loop has three residues of cysteine components and a single residue of proline in each of the connexin proteins. Connexin is very crucial for stabilizing intramolecular activity. Connexins are subcategorized into five families as GJ-A, GJ-B, GJ-C, GJ-D, and GJ-E or they can be referred to as α, β, γ, δ, and ε. These connexin families are categorized based on similarities and differences found in the sequence of amino acids present on the transmembrane protein. The number of connexin proteins present on the transmembrane of the cell depends on the cell type, its species, and its period of development. This can be explained as, on the endoplasmic reticulum, connexins are presently based on the molecule trafficking around the plasma membrane. The mitochondria also have connexin on their membrane and such connexins are expressed as connexin 43. The connexin 43 of the mitochondria membrane is collectively referred to as the mitochondrial connexin 43 (mito Cx43). The connexin 43 is also found to be present on the osteocyte during dendritic and cytoplasm processes performed. These connexin 43 intersect the dendritic cells to scatter and distribute molecules in between cells by forming a close contact during the osteoblast.

Phosphorylation of Connexin:
The lifecycle of a connexin is very complex. Its formation involves stages of transcription of required species of connexin, then followed by the trafficking, and assembly of the particular species of connexin and at the end, synthesis and turnover process of the connexin protein. The internalization of the gap junction and the turnover get linked to the several sites where various events of phosphorylation take place for the formation of the connexin protein. The phosphorylation on connexin reported till now are connexin 32 (Cx32), connexin 43 (Cx43), connexin 45 (Cx45), and connexin 56 (Cx56). Most of the phosphorylation of connexin protein occurs in the region of the C-terminal, except Cx56. Connexin 56 phosphorylated in the region of the cytoplasmic loop, near the C-terminal domain. There is no phosphorylation occurs on the N-terminal region of the connexin. The connexin 26 (Cx26), is the only connexin species that remain in the state of non-phosphorylation. An interesting discovery about Connexin 32 was that they have a half-life of fewer than 5 hours in the Vivo of rodent hepatocytes. And the connexin 43 phosphorylation at different positions may empower the degradation of the gap junction.

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