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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.
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.
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,...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...

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Related Experiment Video

Updated: May 21, 2026

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

Chemokines and the signaling modules regulating integrin affinity.

Alessio Montresor1, Lara Toffali, Gabriela Constantin

  • 1Division of General Pathology, Department of Pathology, University of Verona Verona, Italy.

Frontiers in Immunology
|June 2, 2012
PubMed
Summary

Chemokines regulate leukocyte adhesion by modulating integrin affinity. This study reviews the roles of Rap and Rho small GTPases in integrin activation, offering a modular view of these signaling events.

Keywords:
adhesionchemokineintegrin activationintegrin affinityleukocyte recruitmentrap small GTPasesrho small GTPasessignal transduction

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Last Updated: May 21, 2026

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

Published on: June 13, 2014

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

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12:38

Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction

Published on: February 15, 2018

Area of Science:

  • Cellular Biology
  • Immunology
  • Molecular Biology

Background:

  • Integrin-mediated adhesion is crucial for leukocyte function, involving processes like tethering-rolling and binding stabilization.
  • Arrest chemokines are key regulators of integrin activation, particularly influencing integrin affinity for rapid leukocyte arrest.
  • While signaling pathways are known, their specific role in chemokine-induced integrin affinity modulation in primary leukocytes is less understood.

Purpose of the Study:

  • To summarize the role of Rap and Rho small GTPases in regulating rapid integrin affinity in primary leukocytes.
  • To provide a modular perspective on the pro-adhesive signaling events triggered by arrest chemokines.
  • To discuss potential mechanisms and functional integration of these signaling pathways.

Main Methods:

  • Review of existing literature on integrin-mediated adhesion and chemokine signaling.
  • Analysis of signaling pathways involving Rap and Rho small GTPases in leukocyte integrin activation.
  • Discussion of proposed models for Rho-mediated regulation of cytoskeletal proteins.

Main Results:

  • Rap and Rho small GTPases are central to rapid integrin affinity modulation by arrest chemokines in primary leukocytes.
  • A modular view of these signaling events highlights their distinct and integrated functions.
  • A speculative mechanism for Rho-mediated regulation of cytoskeletal proteins in the final step of integrin activation is proposed.

Conclusions:

  • Rap and Rho GTPases play critical, integrated roles in chemokine-induced integrin activation and leukocyte adhesion.
  • Understanding these signaling modules offers insights into leukocyte trafficking and inflammatory responses.
  • Further research is needed to elucidate the universality and precise mechanisms of these signaling pathways.