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Related Concept Videos

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...
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.
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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,...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
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.
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Corrigendum to "Rap1 organizes lymphocyte front-back polarity via RhoA signaling and talin1" [iScience, Volume 26, Issue 8 (2023) 107292].

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Related Experiment Video

Updated: May 29, 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

Rap1 and integrin inside-out signaling.

Koko Katagiri1, Tatsuo Kinashi

  • 1Department of Life Science, School of Science and Technology, Kansei Gakuin University, Hyogo, Japan. kinashi@takii.kmu.ac.jp

Methods in Molecular Biology (Clifton, N.J.)
|September 13, 2011
PubMed
Summary

Ras proximity 1 (Rap1) regulates integrin-mediated cell adhesion in the immune system. Activated Rap1 enhances leukocyte adhesion to endothelium and antigen-presenting cells, crucial for immune responses.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Signaling

Background:

  • Integrins on leukocytes mediate critical adhesive interactions with other cells and the extracellular matrix.
  • Ras proximity 1 (Rap1) is a signaling molecule emerging as a key regulator of integrin function.
  • Integrin-mediated adhesion is vital for immune cell trafficking, antigen presentation, and effector functions.

Purpose of the Study:

  • To describe methods for studying Ras proximity 1 (Rap1) signaling.
  • To highlight Rap1's role in regulating integrin-mediated cell adhesion.
  • To elucidate Rap1's contribution to immune cell interactions and functions.

Main Methods:

  • Methods for studying Rap1 activation and signaling pathways.
  • Techniques to investigate Rap1's influence on integrin adhesiveness.

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Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
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Last Updated: May 29, 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

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

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07:55

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

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  • Approaches to analyze Rap1-dependent leukocyte adhesion and cell polarity.

    • Main Results:

    • Rap1 activation by stimuli like chemokines and antigens enhances integrin adhesiveness.
    • Rap1 signaling transmits an inside-out signal to integrins, increasing binding to various ligands.
    • Activated Rap1 promotes leukocyte adhesion to endothelium and antigen-presenting cells.
    • Rap1 also induces lymphocyte cell polarity and LFA-1 redistribution.

    Conclusions:

    • Rap1 is a critical regulator of integrin-mediated adhesion in leukocytes.
    • Rap1 signaling is essential for immune cell adhesion, trafficking, and effector functions.
    • Understanding Rap1 pathways offers insights into immune system regulation and potential therapeutic targets.