Related Experiment Video

Updated: Jul 11, 2026

Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion
09:56

Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion

Published on: February 11, 2022

The integrin-growth factor receptor duet

Naved Alam1, Hira Lal Goel, Matthew J Zarif

  • 1Department of Cancer Biology and Cancer Center, University of Massachusetts Medical School, Worcester, Massachusetts, USA.

Journal of Cellular Physiology
|September 22, 2007
PubMed

Insights

Integrins act as molecular switches, controlling growth factor receptor (GFR) activation and cellular responses. This review explores how integrins and GFRs mutually regulate each other for precise cell signaling.

Area of Science:

  • Cellular Biology
  • Molecular Signaling
  • Receptor Interactions

Background:

  • Integrins are crucial cell adhesion receptors regulating cellular processes like growth and differentiation.
  • Integrins interact with growth factor receptors (GFRs) to mediate cellular responses to extracellular signals.

Purpose of the Study:

  • To review the role of integrins as molecular switches in modulating GFR activation and specificity.
  • To examine the reciprocal regulation of integrin function by GFRs and the underlying fine-tuning mechanisms.

Main Methods:

  • Literature review of integrin-GFR interactions.
  • Analysis of molecular mechanisms governing receptor crosstalk.
  • Synthesis of current understanding on integrin and GFR signaling pathways.

Main Results:

  • Integrins act as critical modulators, influencing the activation state and specificity of GFR signaling.
  • GFRs reciprocally regulate integrin activity, impacting cell adhesion and migration.
  • Complex crosstalk mechanisms fine-tune cellular responses to combined integrin and GFR stimulation.

Conclusions:

  • Integrin-GFR interactions are essential for precise control of cellular behavior.
  • Understanding this crosstalk provides insights into cellular signaling and potential therapeutic targets.
  • Further research into these molecular switches can elucidate complex biological processes.

More Related Videos

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs04:15

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs

Published on: February 2, 2024

Preparing a 68Ga-labeled Arginine Glycine Aspartate (RGD)-peptide for Angiogenesis07:48

Preparing a 68Ga-labeled Arginine Glycine Aspartate (RGD)-peptide for Angiogenesis

Published on: January 7, 2019

Related Concept Videos

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,...
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...
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.
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity: