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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 events provide an effective stimulus.

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,...

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Related Experiment Video

Updated: Jul 11, 2026

Imaging Integrin Tension and Cellular Force at Submicron Resolution with an Integrative Tension Sensor

Imaging Integrin Tension and Cellular Force at Submicron Resolution with an Integrative Tension Sensor

Published on: April 25, 2019

Osmosensing by integrins in rat liver.

Freimut Schliess¹, Dieter Häussinger

¹Clinic for Gastroenterology, Hepatology, and Infectiology, Heinrich-Heine-University, Düsseldorf, Germany.

Methods in Enzymology

|September 19, 2007

Summary

Integrins act as osmosensors in liver cells, regulating cell volume, proteolysis, and bile acid excretion. This highlights integrins

Area of Science:

Hepatocyte physiology and cell signaling

Background:

Hepatocyte hydration changes, influenced by osmolarity, hormones, and stress, impact cellular functions.
The perfused rat liver model preserves key in vivo characteristics for studying liver cell behavior.
Cell hydration changes are recognized as triggers for signal transduction pathways controlling liver cell metabolism and stress responses.

Purpose of the Study:

To investigate the role of integrins as osmosensors in the liver.
To elucidate the involvement of integrins in regulating autophagic proteolysis, bile acid excretion, and cell volume.
To determine the function of integrin-mediated signaling in response to hormones like insulin and glutamine.

Main Methods:

Experiments utilizing the perfused rat liver model.
Investigating integrin-dependent signaling pathways, including Src and MAP kinases.

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Analyzing the effects of hypoosmotic swelling on hepatocyte functions.

Main Results:

Integrins function as osmosensors in hepatocytes, mediating responses to osmotic changes.
Integrin signaling inhibits autophagic proteolysis and stimulates canalicular taurocholate excretion.
Hepatocyte swelling, sensed by integrins, is crucial for insulin and glutamine signaling and proteolysis inhibition.

Conclusions:

Integrins play a critical role in sensing cell hydration changes and mediating downstream signaling in hepatocytes.
Integrin-dependent mechanotransduction is integral to growth factor and nutrient signaling pathways.
This research establishes a novel role for integrins in liver cell signaling and response to physiological stimuli.