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Related Concept Videos

Structure of Cadherins01:25

Structure of Cadherins

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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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Cadherins in Tissue Organization01:19

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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.
Cell Sorting During Development
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Catenins01:23

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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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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Cell Adhesion Molecules - Types and Functions01:20

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Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
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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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Related Experiment Video

Updated: Feb 26, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
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Seven pass Cadherins CELSR1-3.

Andre M Goffinet1, Fadel Tissir1

  • 1Université catholique de Louvain, Institute of Neuroscience, UCL/IONS, 73 Avenue Mounier, Box B1.7316, B1200 Brussels, Belgium; FNRS-WELBIO, Belgium.

Seminars in Cell & Developmental Biology
|July 19, 2017
PubMed
Summary
This summary is machine-generated.

Cadherin EGF LAG seven-pass G-type receptors (CELSR1-3) are crucial for epithelial and nervous system development. Further research is needed to understand their signaling pathways, ligands, and roles in disease.

Keywords:
Axon guidanceBrain wiringCiliogenesisNeural tube defectsNeuronal migrationTissue polarity

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Area of Science:

  • Cell Biology
  • Developmental Biology
  • Neuroscience

Background:

  • Cadherin EGF LAG seven-pass G-type receptors (CELSR1-3) are atypical cadherins involved in epithelial and neural functions.
  • CELSR1 is key for epithelial planar cell polarity (PCP), while CELSR2 and CELSR3 are implicated in ciliogenesis and neural development.
  • Mutant mouse studies suggest CELSR proteins interact with FZD3 and FZD6, but their precise roles and signaling mechanisms are not fully understood.

Purpose of the Study:

  • To elucidate the signaling pathways of CELSR1, CELSR2, and CELSR3.
  • To identify putative ligands, particularly WNT factors, that trigger CELSR signaling.
  • To uncover novel intracellular pathways and effectors involved in CELSR signal transduction.

Main Methods:

  • This study involves analyzing existing literature and data on CELSR proteins.
  • Investigating phenotypes in mutant mice to infer protein functions.
  • Focusing on signaling pathway analysis and ligand identification.

Main Results:

  • CELSR1 plays a significant role in epithelial planar cell polarity.
  • CELSR2 and CELSR3 are involved in ciliogenesis and neural development, including neuron migration and axon guidance.
  • Evidence suggests CELSR proteins function in conjunction with FZD3 and FZD6.

Conclusions:

  • CELSR proteins are vital for development and have potential roles in regeneration and disease.
  • Further research is required to fully understand CELSR signaling, including ligand interactions and intracellular effectors.
  • Unraveling these pathways will enhance our knowledge of CELSR functions in health and disease.