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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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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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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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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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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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Mapping and engineering the interaction between adiponectin and T-cadherin.

Roberta Pascolutti1, Sarah C Erlandson1, Dominique J Burri2

  • 1Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, Massachusetts 02115.

The Journal of Biological Chemistry
|January 10, 2020
PubMed
Summary

Researchers elucidated how adiponectin, an anti-diabetic and anti-inflammatory hormone, binds T-cadherin. Structural analysis revealed T-cadherin interacts with adiponectin's globular domain, stabilized by metal ions.

Keywords:
adipokineadiponectincadherincrystallographyprotein engineering

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Adiponectin is a key adipose-derived hormone with pleiotropic effects, including anti-diabetic, anti-inflammatory, and anti-atherosclerotic properties.
  • Adiponectin exists in multiple oligomeric forms and interacts with receptors AdipoR1, AdipoR2, and T-cadherin.
  • The specific binding mechanism between adiponectin and T-cadherin, particularly its high-molecular-weight form, remains incompletely understood.

Purpose of the Study:

  • To elucidate the molecular details of adiponectin's interaction with T-cadherin.
  • To define the structural basis for the specificity of adiponectin binding to T-cadherin.
  • To engineer adiponectin globular domain variants with enhanced T-cadherin binding affinity.

Main Methods:

  • X-ray crystallography was employed to determine the structural basis of the interaction.
  • Protein engineering techniques were utilized to modify the adiponectin globular domain.
  • Binding affinity assays were performed to evaluate engineered variants.

Main Results:

  • T-cadherin specifically binds to the globular domain of adiponectin.
  • Structural stabilization of the adiponectin globular domain by bound metal ions is crucial for T-cadherin binding.
  • Engineered adiponectin globular domain variants demonstrated enhanced binding affinity for T-cadherin.

Conclusions:

  • The study defines the molecular basis for adiponectin-T-cadherin interaction, highlighting the role of the globular domain and metal ion stabilization.
  • Engineered adiponectin globular domain variants represent valuable tools for further research into adiponectin's biological functions.
  • These findings contribute to understanding adiponectin's role in cardiovascular health and metabolic regulation.