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Related Concept Videos

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,...
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.
Anchoring Junctions01:03

Anchoring Junctions

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:...
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...
Selectins01:25

Selectins

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, which...

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Related Experiment Video

Updated: May 18, 2026

A 3D Spheroid Model as a More Physiological System for Cancer-Associated Fibroblasts Differentiation and Invasion In Vitro Studies
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A 3D Spheroid Model as a More Physiological System for Cancer-Associated Fibroblasts Differentiation and Invasion In Vitro Studies

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α3β1 integrins regulate CD151 complex assembly and membrane dynamics in carcinoma cells within 3D environments.

T M E Scales1, A Jayo, B Obara

  • 1Randall Division of Cell and Molecular Biophysics, King's College London, New Hunts House, Guys Campus, London, UK.

Oncogene
|September 19, 2012
PubMed
Summary

Integrins like α3β1 and tetraspanin CD151 directly associate in migrating breast cancer cells, regulating tumor invasion. This crosstalk impacts cell polarity and invasion in 3D environments.

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08:08

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Revealing the Cytoskeletal Organization of Invasive Cancer Cells in 3D
11:09

Revealing the Cytoskeletal Organization of Invasive Cancer Cells in 3D

Published on: October 26, 2013

Area of Science:

  • Cell biology
  • Molecular biology
  • Cancer research

Background:

  • Integrins (ECM receptors) and tetraspanins are crucial in tumor cell invasion.
  • The integrin α3β1 and tetraspanin CD151 cooperate in carcinoma cell adhesion and migration.
  • Spatial and temporal regulation of crosstalk between these proteins in intact cells is poorly understood.

Purpose of the Study:

  • To investigate the direct association between α3β1 integrin and CD151 in polarized migrating breast carcinoma cells.
  • To understand the functional consequences of this interaction on cell polarity, invasion, and signaling.

Main Methods:

  • Fluorescence resonance energy transfer (FRET) to detect protein associations in live cells.
  • Utilized 2D and 3D cell culture models with laminin and matrigel.
  • Employing gene silencing (α3-silencing) to assess the role of α3β1 integrin.

Main Results:

  • Demonstrated direct association between α3β1 and CD151 at the leading and trailing edges of migrating breast carcinoma cells.
  • Observed that localized α3β1-CD151 binding correlates with reduced CD151 homodimerization.
  • Showed that loss of α3β1 integrin increases CD151 homodimerization, Rho GTPase activation, and decreases cell polarity and invasion in 3D ECM.

Conclusions:

  • α3β1 and CD151 dynamically associate in specific subcellular locations to regulate GTPase signaling and promote tumor cell invasion.
  • This crosstalk is essential for establishing cell polarity and driving invasion in 3D environments.
  • Findings reveal novel insights into receptor complex dynamics during cancer cell invasion.