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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.
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Invadosome is a broad category of cell surface structures with proteolytic activity that  degrades the extracellular matrix (ECM). Invadosomes are present in normal cell types, including macrophages, endothelial cells, and neurons, as well as tumor cells. Although the macrophage podosomes and tumor cell invadopodia are classified as invadosomes, they have different structures, molecular pathways, and functions. Podosomes are short structures that last for a few minutes. However, invadopodia can...
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Cell Migration01:19

Cell Migration

Cell migration is a process by which the cells move from one location to another, playing an essential role in embryological development, repair and regeneration, immune response, and metastasis. Cells migrate in response to chemical or mechanical signals generated by specific organs or tissues. The overall mechanism includes three steps - polarization, protrusion, and release. Polarization involves the formation of a distinct cell front and rear, which determines the direction of movement.
Cell Migration01:09

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Cell migration, the process by which cells move from one location to another, is essential for the proper development and viability of organisms throughout their life. When cells are not able to migrate properly to their ordained locations, various disorders may occur. For example, disruption in cell migration causes chronic inflammatory diseases such as arthritis.

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Related Experiment Video

Updated: Jul 14, 2026

An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers
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uPAR-induced cell adhesion and migration: vitronectin provides the key.

Chris D Madsen1, Gian Maria Sarra Ferraris, Annapaola Andolfo

  • 1FIRC Institute of Molecular Oncology (IFOM), 20139 Milan, Italy.

The Journal of Cell Biology
|June 6, 2007
PubMed
Summary

The urokinase plasminogen activator receptor (uPAR) directly binds vitronectin, initiating cell shape and migration changes. This interaction is crucial for cancer progression, independent of other protein interactions.

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Published on: May 8, 2012

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • The urokinase plasminogen activator receptor (uPAR) is a membrane receptor implicated in cancer malignancy.
  • uPAR expression influences cell morphology and migration, key processes in cancer progression.

Purpose of the Study:

  • To identify the specific molecular interactions of uPAR essential for its function in cell morphology and migration.
  • To elucidate the mechanism by which uPAR regulates cellular behavior.

Main Methods:

  • A comprehensive functional alanine scan of uPAR was performed in HEK293 cells.
  • Characterization of 255 mutant uPAR receptors to assess their impact on cell morphology and binding.
  • Utilized a membrane-tethered plasminogen activator inhibitor-1 as a control for uPAR-vitronectin interactions.

Main Results:

  • 34 out of 255 uPAR mutants failed to induce changes in cell morphology.
  • These mutants exhibited a specific defect in integrin-independent cell binding to vitronectin.
  • A membrane-tethered plasminogen activator inhibitor-1 mimicked uPAR-induced changes, confirming the uPAR-vitronectin interaction's role.

Conclusions:

  • A direct interaction between uPAR and vitronectin is both necessary and sufficient for initiating downstream cellular changes.
  • uPAR modulates cell-matrix interactions to evoke complex cellular responses, including changes in morphology and migration.
  • This study reveals a novel mechanism where a cell adhesion molecule, without intrinsic signaling, drives cellular behavior by altering cell-matrix contact.