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Related Concept Videos

Integrins01:10

Integrins

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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.
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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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Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
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Activation of Integrins01:15

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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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Selectins01:25

Selectins

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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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Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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Related Experiment Video

Updated: Dec 2, 2025

Preparing a 68Ga-labeled Arginine Glycine Aspartate RGD-peptide for Angiogenesis
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αv-Class integrin binding to fibronectin is solely mediated by RGD and unaffected by an RGE mutation.

María Benito-Jardón1,2, Nico Strohmeyer3, Sheila Ortega-Sanchís1,2

  • 1Department of Biochemistry and Molecular Biology, Universitat de València, Burjassot, Spain.

The Journal of Cell Biology
|November 3, 2020
PubMed
Summary
This summary is machine-generated.

Fibronectin

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Extracellular Matrix Research

Background:

  • Fibronectin (FN) is a key extracellular matrix glycoprotein.
  • FN mediates cell adhesion and fibril network assembly.
  • The RGD motif is crucial for FN-integrin interactions and fibrillogenesis.

Purpose of the Study:

  • To investigate if the RGD motif is the only binding site for αv-class integrins on fibronectin.
  • To resolve conflicting in vitro and in vivo data regarding FN-RGE binding.
  • To elucidate the role of specific FN motifs in integrin binding and fibril formation.

Main Methods:

  • Single-cell force spectroscopy to probe molecular interactions.
  • Engineered cell lines to study specific fibronectin variants.
  • Generation and analysis of RGD motif-deficient mice (Fn1ΔRGD/ΔRGD).

Main Results:

  • α5β1 and αv-class integrins exclusively bind the FN-RGD motif.
  • αv-class integrins, but not α5β1, retain binding to the FN-RGE variant.
  • Fn1ΔRGD/ΔRGD tissues exhibit defective fibronectin fibril assembly in a syndecan-dependent manner.

Conclusions:

  • The FN-RGD motif is essential for α5β1 and αv-class integrin binding and normal fibrillogenesis.
  • The FN-RGE motif retains functionality for αv-class integrin binding.
  • Syndecans play a critical role in fibronectin fibril assembly involving the RGD motif.