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Activation of Integrins

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...

Intracellular Signaling Affects Focal Adhesions

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...

Integrins

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,...

Anchoring Junctions

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:...

Adherens Junctions

Adherens Junctions

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

Tension Response at Adherens Junctions

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...

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Related Experiment Video

Updated: Jun 7, 2025

Sensing of Barrier Tissue Disruption with an Organic Electrochemical Transistor

Sensing of Barrier Tissue Disruption with an Organic Electrochemical Transistor

Published on: February 10, 2014

Apical integrins as a switchable target to regulate the epithelial barrier.

Raven J Peterson¹, Ryan C Reed¹, Colin R Zamecnik²

¹Division of Pulmonary, Allergy, Critical Care and Sleep Medicine, Department of Medicine, Emory University School of Medicine, Atlanta, GA 30322, USA.

Journal of Cell Science

|November 18, 2024

Summary

Apical integrins regulate epithelial barrier function in a conformation-specific manner. Targeting closed integrins increases permeability, while open integrins decrease it, revealing a novel regulatory mechanism.

Keywords:

Claudin Epithelium Integrin Paracellular permeability Tight junction ZO-1

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Related Experiment Videos

Last Updated: Jun 7, 2025

Sensing of Barrier Tissue Disruption with an Organic Electrochemical Transistor

Sensing of Barrier Tissue Disruption with an Organic Electrochemical Transistor

Published on: February 10, 2014

Investigating Intestinal Barrier Breakdown in Living Organoids

Investigating Intestinal Barrier Breakdown in Living Organoids

Published on: March 26, 2020

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

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

Published on: March 8, 2017

Area of Science:

Cell Biology
Epithelial Biology
Biophysics

Background:

Tight junctions are crucial for epithelial barrier function.
Apical integrins are potential regulators, but their role is indirectly measured.
Understanding integrin conformation's impact on barrier is needed.

Purpose of the Study:

To investigate the conformation-specific regulation of epithelial barrier function by apical integrins.
To elucidate the molecular mechanisms underlying integrin-mediated barrier modulation.

Main Methods:

Utilized polymeric nanowires conjugated with anti-integrin β1 antibodies to target specific integrin conformations.
Assessed epithelial permeability and junctional protein morphology (ZO-1, claudins).
Investigated the involvement of myosin light chain kinases (MLCKs) and Rho kinases (ROCKs), actin, and talin.

Main Results:

Targeting closed integrins increased epithelial permeability and induced ruffling of ZO-1, claudin-2, and claudin-4.
Ruffling was dependent on MLCKs and ROCKs.
Targeting open integrins decreased permeability and linearized junctions.
Integrin targeting differentially affected actin and talin.

Conclusions:

Apical integrins act as conformation-sensitive switches regulating epithelial barrier function.
Integrin conformation dictates whether the barrier is increased or decreased.
This provides a novel mechanism for controlling epithelial permeability.