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Related Concept Videos

Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

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The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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Adherens Junctions

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Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
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Catenins01:23

Catenins

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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
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The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
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Cadherin Regulation of Endoplasmic Reticulum-Plasma Membrane Contact Sites.

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    Adherens junctions recruit endoplasmic reticulum (ER) tubules to cell junctions, forming ER-plasma membrane contact sites. This complex integrates cell mechanics and plasma membrane homeostasis, impacting cellular lipid levels.

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    Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
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    Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

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    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • The endoplasmic reticulum (ER) is a dynamic organelle involved in lipid synthesis and protein folding.
    • ER tubule organization influences interactions with other organelles and the plasma membrane.
    • Previous studies noted ER tubule association with desmosomes, but the recruitment mechanism was unknown.

    Purpose of the Study:

    • To elucidate the mechanism of ER tubule recruitment to intercellular junctions.
    • To investigate the role of adherens junctions in ER positioning.
    • To understand the functional implications of ER-plasma membrane contact sites.

    Main Methods:

    • Cell culture and live imaging techniques.
    • Immunofluorescence microscopy to visualize junctional proteins and ER.
    • Genetic manipulation to ablate adherens junction components.

    Main Results:

    • Adherens junctions recruit ER tubules to nascent cell-cell contacts.
    • This recruitment is dependent on E-cadherin, α-catenin, and vinculin.
    • A tripartite complex of adherens junctions, ER-plasma membrane contact sites (ER-PMCS), and desmosomes is formed.
    • Ablation of adherens junctions disrupts this complex and alters cellular lipid levels.

    Conclusions:

    • Cadherins are key regulators of ER-PMCS positioning.
    • The adherens junction-ER-PMCS-desmosome complex integrates mechanical signaling with plasma membrane homeostasis.
    • ER recruitment to cell junctions is crucial for maintaining cellular lipid balance.