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Related Concept Videos

Immunoglobulin-like Cell Adhesion Molecules01:31

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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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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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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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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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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Related Experiment Video

Updated: Mar 7, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
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Calcineurin for T cell adhesion.

John F Foley1

  • 1Science Signaling, AAAS, Washington, DC 20005, USA.

Science Signaling
|February 9, 2017
PubMed
Summary
This summary is machine-generated.

The phosphatase calcineurin activates transcription factors and enhances T cell adhesion during T cell activation. This dual role is crucial for immune responses.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • Calcineurin is a key calcium-dependent phosphatase involved in immune cell signaling.
  • T cell activation triggers complex downstream events, including gene transcription and cellular interactions.

Purpose of the Study:

  • To elucidate the multifaceted roles of calcineurin in T cell activation.
  • To investigate calcineurin's involvement in both transcriptional regulation and cell adhesion.

Main Methods:

  • Utilized molecular biology techniques to study calcineurin activity.
  • Employed cell-based assays to assess T cell activation markers and adhesion properties.

Main Results:

  • Calcineurin was confirmed to activate specific transcription factors essential for T cell function.
  • Evidence demonstrated that calcineurin directly promotes T cell adhesion following activation.

Conclusions:

  • Calcineurin plays a critical dual role in T cell activation, regulating both gene expression and cell-cell interactions.
  • Understanding calcineurin's functions provides insights into T cell-mediated immunity and potential therapeutic targets.