Adherens Junction Proteins
E-Cadherin
A key function of the cell-cell adhesion protein E-cadherin in epithelial development. E-cadherin may be a powerful breast cancer invader/tumor suppressor, according to data from model systems. A poor prognosis in breast cancer patients has been observed to be correlated with partial or complete loss of E-cadherin expression, which is consistent with this involvement in the development of the disease. Human chromosome 16q22.1 contains the E-cadherin gene (CDH1), a region that is frequently impacted by the loss of heterozygosity in sporadic breast cancer. Loss of heterozygosity of the wild-type CDH1 allele occurs frequently in invasive lobular breast carcinomas, which are typically entirely E-cadherin-negative.
E-Catenin
High levels of -E-catenin are found in the adherens junction of the cardiac intercalated disc, and changes in this protein’s expression are linked to dilated cardiomyopathy, a condition that has been linked to and proved to affect the cytoskeleton. We anticipated that since -E-catenin is dynamically related to the cytoskeleton in other cell types, it would be crucial for cardiac adherens junction ultrastructure and function in the heart in vivo. We used a conditional strategy to investigate the functional significance of -catenin in the heart because it is universally expressed and essential for early vertebrate embryonic development. We created myosin light chain 2 (MLC2v)-Cre knock-in mice with the special ability to produce cardiomyocyte-specific -E-catenin conditional knockout (cKO) mice.
α-Catenin
α-catenin has a wide range of functions and is involved in the development of embryos and tissues, cell migration, and differentiation (i.e. commitment to a certain cell type) (reviewed in α-catenin is strenuous at cell-cell adhesion sites, such as tight junctions and adherens junctions, through its association with a related family member, beta-catenin. This binding interaction is controlled by the phosphorylation of either – or -catenin, and phosphorylated β-catenin is anticipated to compete with the homodimerization of α-catenin. Contrary to the monomer, which prefers E-cadherin β-catenin complexes, dimerization of α-catenin results in a complex with functional domains at both ends that bind actin filaments preferentially.
Adherens Junction
The adherens junction (AJ), a component of the cell-cell junction, is where cadherin receptors operate to homophilically connect the nearby plasma membranes. The cytoplasmic proteins known as catenins, with which cadherins are associated, then bind to the cytoskeletal elements actin filaments and microtubules. The interaction of these chemical complexes with additional proteins, such as signaling molecules, transforms the AJs into extremely dynamic and controllable structures. The morphogenesis and remodeling of tissues and organs depend on the regulation of cell-cell interactions as well as the physical connecting of cells, both of which are facilitated by AJs of this type. Therefore, understanding the AJs’ molecular architecture and their regulation processes is essential to comprehend how the multicellular system is structured.
Over a set of specified processes, such as initiation, cadherin recruitment, and the recruitment of plaque proteins, the creation and operation of the adherens junction may be explained. When migrating cells first come into contact with one another to form a tissue, for example, adherens junction assembly takes place. It can also happen in pre-existing tissues when cells divide, change shape, or move in response to biochemical or mechanical stimuli. Initiation of adherens junctions during embryonic morphogenesis and in cell culture at the point at which migrating cells first come into contact have been extensively studied. The formation and dissolution of AJs occur throughout life, not just during development, and this turnover is essential for maintaining the homeostasis of epithelial tissues.
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