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Related Concept Videos

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,...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Proteomic analysis of integrin adhesion complexes.

Adam Byron1, Jonathan D Humphries, Mark D Bass

  • 1Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, UK.

Science Signaling
|April 7, 2011
PubMed
Summary
This summary is machine-generated.

Researchers developed a new method to study cell adhesion complexes. This technique identified regulator of chromosome condensation-2 (RCC2) in fibronectin signaling, advancing our understanding of cell movement.

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Area of Science:

  • Cell biology
  • Molecular biology
  • Proteomics

Background:

  • Integrin receptors are key regulators of cell fate, linking extracellular matrix interactions to intracellular signaling.
  • Understanding the molecular composition of integrin adhesion complexes is crucial for deciphering cell behavior.
  • Previous methods struggled to analyze these labile and inaccessible signaling complexes.

Purpose of the Study:

  • To develop a novel proteomics methodology for isolating and analyzing ligand-induced integrin adhesion complexes.
  • To define the core and receptor-specific subnetworks within these complexes.
  • To identify novel components involved in integrin-mediated signaling.

Main Methods:

  • Development of a technique to isolate ligand-induced integrin adhesion complexes.
  • Proteomic analysis of isolated complexes from various receptor-ligand pairs.
  • Bioinformatic analysis to define core and specific subnetworks.

Main Results:

  • Successfully isolated and analyzed integrin adhesion complexes.
  • Defined core and receptor-specific subnetworks, revealing complex organization.
  • Identified regulator of chromosome condensation-2 (RCC2) as a novel component in fibronectin signaling pathways.
  • RCC2 was implicated in regulating directional cell movement.

Conclusions:

  • The developed proteomics pipeline enables comprehensive investigation of adhesion complex composition.
  • This approach provides new insights into the molecular mechanisms controlling cell morphology, survival, movement, and differentiation.
  • The identification of RCC2 highlights its role in integrin-mediated directional cell migration.