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Gap junction
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Gap junction
Gap junctions are membrane channels between adjacent cells that allow the direct exchange of cytoplasmic substances, such as small molecules, substrates, and metabolites.
Gap junctions were first described as close appositions alongside tight junctions, however, electron microscopy studies in 1967 led to gap junctions being named as such to be distinguished from tight junctions. They bridge a 2-4 nm gap between cell membranes.
Gap junctions use protein complexes known as connexons, composed of connexin proteins to connect one cell to another. Gap junction proteins include the more than 26 types of connexin, as well as at least 12 non-connexin components that make up the gap junction complex or nexus, including the tight junction protein ZO-1—a protein that holds membrane content together and adds structural clarity to a cell, sodium channels, and aquaporin.
More gap junction proteins have become known due to the development of next-generation sequencing. Connexins were found to be structurally homologous between vertebrates and invertebrates but different in sequence. As a result, the term innexin is used to differentiate invertebrate connexins. There are more than 20 known innexins, along with unnexins in parasites and vinnexins in viruses.
An electrical synapse is a gap junction that can transmit action potentials between neurons. Such synapses create bidirectional continuous-time electrical coupling between neurons. Connexon pairs act as generalized regulated gates for ions and smaller molecules between cells. Hemichannel connexons form channels to the extracellular environment.
A gap junction or macula communicans is different from an ephaptic coupling that involves electrical signals external to the cells.
In vertebrates, gap junction hemichannels are primarily homo- or hetero-hexamers of connexin proteins. Hetero-hexamers at gap junction plaques, help form a uniform intercellular space of 2-4 nm. In this way hemichannels in the membrane of each cell are aligned with one another forming an intercellular communication path.
Invertebrate gap junctions comprise proteins from the innexin family. Innexins have no significant sequence homology with connexins. Though differing in sequence to connexins, innexins are similar enough to connexins to form gap junctions in vivo in the same way connexins do.
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Gap junction
Gap junctions are membrane channels between adjacent cells that allow the direct exchange of cytoplasmic substances, such as small molecules, substrates, and metabolites.
Gap junctions were first described as close appositions alongside tight junctions, however, electron microscopy studies in 1967 led to gap junctions being named as such to be distinguished from tight junctions. They bridge a 2-4 nm gap between cell membranes.
Gap junctions use protein complexes known as connexons, composed of connexin proteins to connect one cell to another. Gap junction proteins include the more than 26 types of connexin, as well as at least 12 non-connexin components that make up the gap junction complex or nexus, including the tight junction protein ZO-1—a protein that holds membrane content together and adds structural clarity to a cell, sodium channels, and aquaporin.
More gap junction proteins have become known due to the development of next-generation sequencing. Connexins were found to be structurally homologous between vertebrates and invertebrates but different in sequence. As a result, the term innexin is used to differentiate invertebrate connexins. There are more than 20 known innexins, along with unnexins in parasites and vinnexins in viruses.
An electrical synapse is a gap junction that can transmit action potentials between neurons. Such synapses create bidirectional continuous-time electrical coupling between neurons. Connexon pairs act as generalized regulated gates for ions and smaller molecules between cells. Hemichannel connexons form channels to the extracellular environment.
A gap junction or macula communicans is different from an ephaptic coupling that involves electrical signals external to the cells.
In vertebrates, gap junction hemichannels are primarily homo- or hetero-hexamers of connexin proteins. Hetero-hexamers at gap junction plaques, help form a uniform intercellular space of 2-4 nm. In this way hemichannels in the membrane of each cell are aligned with one another forming an intercellular communication path.
Invertebrate gap junctions comprise proteins from the innexin family. Innexins have no significant sequence homology with connexins. Though differing in sequence to connexins, innexins are similar enough to connexins to form gap junctions in vivo in the same way connexins do.
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