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Related Concept Videos

Integrins01:10

Integrins

4.8K
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,...
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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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Activation of Integrins01:15

Activation of Integrins

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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."
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...
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Anchoring Junctions01:03

Anchoring Junctions

4.2K
Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
4.2K
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

3.3K
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...
3.3K
Adherens Junctions01:24

Adherens Junctions

5.8K
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
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Related Experiment Video

Updated: Apr 27, 2026

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of &#946;2 Integrin Activation
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Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation

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α2β1 Integrin.

Aasakiran Madamanchi1, Samuel A Santoro, Mary M Zutter

  • 1Department of Pathology, Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN, USA.

Advances in Experimental Medicine and Biology
|July 16, 2014
PubMed
Summary

The α2β1 integrin (VLA-2) acts as a crucial receptor for various molecules, influencing platelet function, immunity, cancer, and development. Its structural motifs and conformational states are key to its diverse biological roles.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • The α2β1 integrin, also known as VLA-2, is recognized as a receptor for extracellular matrix components like collagens and laminins.
  • It also binds to numerous other matrix and non-matrix molecules, highlighting its versatile role.
  • Its structure and function are critical in various physiological and pathological processes.

Purpose of the Study:

  • To elucidate the structural motifs of the α2 I domain essential for ligand binding.
  • To define the distinct conformations of α2β1 integrin that regulate ligand binding activity.
  • To review the critical role of α2β1 integrin in platelet function, homeostasis, immunity, cancer, and development.

Main Methods:

  • Extensive structural analyses of the α2 I domain.

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

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Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
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Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads

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  • In vitro and in vivo experiments to define mechanisms of action.
  • Review of genetic and epidemiologic studies.

    • Main Results:

    • Detailed understanding of α2 I domain structural motifs for ligand binding.
    • Identification of inactive, partially active, and highly active ligand-binding conformations.
    • Elucidation of α2β1 integrin's critical role in platelet function and homeostasis.

    Conclusions:

    • α2β1 integrin is a multifunctional receptor with significant roles in diverse biological processes.
    • Its structural and conformational properties dictate its broad range of ligand interactions.
    • Genetic and epidemiological data confirm its involvement in human physiology and disease states, including immunity, cancer, and development.