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Related Concept Videos

Adherens Junctions01:24

Adherens Junctions

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.
Adherens Junctions are Dynamic
The endothelial cells...
Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
Structure of Cadherins01:25

Structure of Cadherins

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 diversity of cadherins...
Catenins01:23

Catenins

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.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

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.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...

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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Nectin ectodomain structures reveal a canonical adhesive interface.

Oliver J Harrison1, Jeremie Vendome, Julia Brasch

  • 1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York, USA.

Nature Structural & Molecular Biology
|August 21, 2012
PubMed
Summary
This summary is machine-generated.

Nectins are cell adhesion proteins. This study reveals their structures and how they bind, explaining how these immunoglobulin superfamily glycoproteins mediate tissue patterning through specific interactions.

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Area of Science:

  • Molecular and Cellular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Nectins are immunoglobulin superfamily glycoproteins crucial for intercellular adhesion in vertebrate tissues.
  • Nectin interactions, both homophilic and heterophilic, play a role in tissue patterning.
  • Understanding nectin binding mechanisms is key to deciphering their biological functions.

Purpose of the Study:

  • To determine the homophilic binding affinities and heterophilic specificities of human and mouse nectins and nectin-like 5 (Necl-5).
  • To elucidate the molecular basis of nectin adhesion and specificity through structural analysis.
  • To clarify the nature of nectin dimerization in adhesive interactions.

Main Methods:

  • Measurement of homophilic binding affinities and heterophilic specificities for nectins and Necl-5.
  • Determination of crystal structures of full ectodomains or adhesive fragments of nectins and Necl-5.
  • Cross-linking experiments to validate the functional relevance of observed dimeric interfaces.

Main Results:

  • A comprehensive profile of homophilic binding strengths and heterophilic specificities was established for nectins and Necl-5.
  • Crystal structures revealed nectins forming dimers through a conserved interface.
  • Evidence supports this conserved interface representing the functional adhesive trans interaction, not a cis dimer.

Conclusions:

  • The determined structures provide a direct molecular explanation for the adhesive binding specificity of nectins.
  • The study clarifies the dimeric interaction mode of nectins as crucial for their adhesive function.
  • These findings enhance our understanding of nectin-mediated cell adhesion and its role in tissue organization.