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Activation of Integrins01:15

Activation of Integrins

5.3K
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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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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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.
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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IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Adherens Junctions01:24

Adherens Junctions

6.9K
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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Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

4.5K
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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Related Experiment Video

Updated: Feb 25, 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

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Integrin αIIbβ3 outside-in signaling.

Tom N Durrant1, Marion T van den Bosch1, Ingeborg Hers1

  • 1School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, United Kingdom.

Blood
|August 11, 2017
PubMed
Summary

Integrin αIIbβ3, a key platelet receptor, mediates hemostasis and thrombosis. This review details its complex outside-in signaling pathways, crucial for platelet function and clot formation.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Hematology

Background:

  • Integrin αIIbβ3 is a critical platelet receptor involved in hemostasis and thrombosis.
  • It mediates bidirectional signaling across the plasma membrane, essential for platelet activation and function.

Purpose of the Study:

  • To provide a comprehensive overview of αIIbβ3 outside-in signaling.
  • To identify key signaling players and their cooperative mechanisms.
  • To highlight current knowledge gaps and future research directions.

Main Methods:

  • Literature review of integrin biology and platelet signaling.
  • Analysis of molecular mechanisms in αIIbβ3 outside-in signaling.
  • Synthesis of information on key signaling components and pathways.

Main Results:

  • αIIbβ3 outside-in signaling is a complex process involving numerous enzymes, adaptors, and cytoskeletal elements.
  • Ligand binding and integrin clustering trigger downstream signaling cascades.
  • These cascades amplify cellular events like platelet spreading and clot retraction.

Conclusions:

  • Understanding αIIbβ3 outside-in signaling is vital for comprehending platelet biology.
  • Further research is needed to fully elucidate the intricate network of signaling components.
  • This knowledge can inform therapeutic strategies for bleeding and clotting disorders.