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Related Concept Videos

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.
Catenins in Cell Junctions
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Tension Response at Adherens Junctions01:26

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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.
α-Catenin as a Mechanosensory Protein
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Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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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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Cell sorting plays an...
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Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

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In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
Anchoring junctions mechanically attach a cell to the...
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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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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.
Some...
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Related Experiment Video

Updated: Apr 16, 2026

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
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Tenascin-X: beyond the architectural function.

Ulrich Valcourt1, Lindsay B Alcaraz, Jean-Yves Exposito

  • 1a Inserm U1052, Centre de Recherche en Cancérologie de Lyon , Lyon , France.

Cell Adhesion & Migration
|March 21, 2015
PubMed
Summary

Tenascin-X (TN-X) is a key extracellular matrix protein crucial for tissue structure and cell adhesion. Emerging research reveals its role in regulating signaling pathways like TGF-β, impacting cell plasticity.

Keywords:
ECM, extracellular matrixEDS, Ehlers-Danlos syndromeEGF, epidermal growth factorEMT, epithelial-to-mesenchymal transitionEhlers-Danlos syndrome (EDS)FAK, focal adhesion kinaseFBG, fibrinogen-like domainFNIII, fibronectin type III moduleLAP, latency associated peptideMMP, matrix metalloproteinaseSLC, small latent complexTGF-βTGF-β activationTN, tenascinTSP-1, thrombospondin-1VEGF, vascular endothelial growth factorcell signalingepithelial-to-mesenchymal transition (EMT)integrin α11β1matricellular proteintenascin-Xtransforming growth factor-β

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Area of Science:

  • Extracellular matrix biology
  • Molecular and cell biology
  • Connective tissue disorders

Background:

  • Tenascin-X (TN-X) is the largest glycoprotein in the tenascin (TN) family, essential for extracellular matrix structure.
  • Loss-of-function mutations in TN-X cause a connective tissue disorder, highlighting its critical architectural role.
  • TN-X also functions as a matricellular protein, modulating cell adhesion and potentially regulating signaling pathways.

Purpose of the Study:

  • To elucidate the cellular functions associated with the anti-adhesive properties of Tenascin-X.
  • To investigate the role of TN-X as an extracellular regulator of signaling pathways.
  • To determine if TN-X's signaling functions are linked to its matricellular properties.

Main Methods:

  • The study likely involved analyzing genetic data from patients with connective tissue disorders.
  • In vitro experiments using cell cultures to assess cell adhesion and migration modulated by TN-X.
  • Biochemical assays to investigate the interaction of TN-X with signaling molecules like TGF-β.

Main Results:

  • Tenascin-X loss-of-function leads to connective tissue disorders, confirming its architectural importance.
  • TN-X exhibits anti-adhesive properties, though its specific cellular functions remain to be fully elucidated.
  • Evidence suggests TN-X regulates Transforming Growth Factor (TGF)-β bioavailability and modulates epithelial cell plasticity.

Conclusions:

  • Tenascin-X is vital for both tissue architecture and cell behavior.
  • Further research is needed to connect TN-X's matricellular functions with its newly identified roles in extracellular signaling.
  • Understanding these links could reveal new therapeutic targets for connective tissue disorders and cancer.