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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,...
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.
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...
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...
Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
The Integrin family of proteins is primarily  involved in a...

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Related Experiment Video

Updated: Jun 21, 2026

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
07:55

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

Published on: March 8, 2017

Evolution of complexity in the integrin adhesome.

Ronen Zaidel-Bar1

  • 1Department of Zoology, University of Wisconsin-Madison, Madison, WI 53706, USA. zaidelbar@gmail.com

The Journal of Cell Biology
|August 12, 2009
PubMed
Summary

The study reveals that key signaling proteins predated integrins, with complexity arising through gene duplication and new interactions, enhancing cell adhesion specificity over evolutionary time.

Area of Science:

  • Evolutionary biology
  • Cell biology
  • Biochemistry

Background:

  • Integrin-mediated adhesion is fundamental to multicellular life.
  • The evolutionary origins and diversification of the adhesome remain incompletely understood.

Purpose of the Study:

  • To investigate the evolutionary conservation and expansion of adhesome proteins across diverse model organisms.
  • To understand the co-evolution of integrins with signaling pathways.

Main Methods:

  • Comparative genomic analysis of 192 adhesome proteins in nine model organisms.
  • Tracing the evolutionary history of protein families and domains.
  • Analyzing the expansion of specific functional groups and protein-protein interactions.

Main Results:

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

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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

Related Experiment Videos

Last Updated: Jun 21, 2026

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
07:55

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

Published on: March 8, 2017

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

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

  • Rho GTPases, kinases, and phosphatases predate integrins; tyrosine phosphorylation emerged with integrins.
  • Significant expansion of GAPs, GEFs, adaptors, and receptors, alongside domains like SH3, PH, and SH2, driven by gene duplication.
  • Paralogues exhibit distinct interaction partners, increasing signaling specificity and repertoire.
  • Protein interaction number correlates positively with evolutionary age.

Conclusions:

  • Adhesome complexity evolved through gene duplication and the creation of novel interactions.
  • This evolutionary trajectory enhanced integrin-mediated signaling specificity.
  • The findings provide a framework for studying integrin adhesion in simpler model systems.