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Related Concept Videos

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.
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...
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,...
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...
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...
What is Cell Signaling?02:03

What is Cell Signaling?

Despite the protective membrane that separates a cell from the environment, cells need the ability to detect and respond to environmental changes. Additionally, cells often need to communicate with one another. Unicellular and multicellular organisms use a variety of cell signaling mechanisms to communicate to respond to the environment.

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Related Experiment Video

Updated: May 27, 2026

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

Integrin inside-out signaling and the immunological synapse.

Timothy A Springer1, Michael L Dustin

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Immune Disease Institute and Children's Hospital, Boston, MA 02115, United States. springer_lab@idi.harvard.edu

Current Opinion in Cell Biology
|December 2, 2011
PubMed
Summary

Integrins switch between bent and extended states, with only the extended-open conformation enabling high-affinity cell adhesion. This conformational change is crucial for integrin function in processes like the immunological synapse.

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Last Updated: May 27, 2026

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

An Endothelial Planar Cell Model for Imaging Immunological Synapse Dynamics
09:25

An Endothelial Planar Cell Model for Imaging Immunological Synapse Dynamics

Published on: December 24, 2015

Imaging the Human Immunological Synapse
09:37

Imaging the Human Immunological Synapse

Published on: December 26, 2019

Area of Science:

  • Cell biology
  • Biochemistry
  • Biophysics

Background:

  • Integrins are cell surface receptors mediating cell adhesion.
  • Integrins exist in different conformational states affecting ligand binding affinity.
  • Understanding integrin conformational dynamics is key to cell signaling.

Purpose of the Study:

  • To elucidate the conformational states of integrins.
  • To define the structural basis for high-affinity ligand binding.
  • To investigate the role of integrin conformation in cell adhesion.

Main Methods:

  • Analysis of integrin conformational states (bent vs. extended, closed vs. open headpiece).
  • Characterization of allosteric communication within the βI domain.
  • Investigation of integrin-ligand interactions (e.g., LFA-1-ICAM-1).

Main Results:

  • Integrins equilibrate between bent-closed, extended-closed, and extended-open states.
  • Headpiece opening involves significant structural rearrangements, including hybrid domain swing-out.
  • Extended-open integrins exhibit 10^3-10^4 fold higher affinity than other states.
  • High-affinity binding is essential for integrin-mediated adhesion, as seen in LFA-1-ICAM-1 interactions.

Conclusions:

  • Integrin conformation dictates ligand-binding affinity and adhesion function.
  • The extended-open state is critical for physiological integrin-mediated adhesion.
  • Allosteric mechanisms within the βI domain regulate integrin affinity and function.