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Intracellular Signaling Affects Focal Adhesions01:17

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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.
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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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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:...
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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...
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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
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Lfc subcellular localization and activity is controlled by αv-class integrin.

Georgina P Coló1, Andrea Seiwert1, Raquel B Haga1

  • 1Department of Molecular Medicine, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.

Journal of Cell Science
|May 2, 2023
PubMed
Summary
This summary is machine-generated.

Fibronectin (FN)-binding integrins regulate cellular responses. FN-bound αvβ3 integrin, via Lfc, activates RhoA, impacting cell structure and focal adhesions.

Keywords:
Actin dynamicsFibronectinGEF-H1IntegrinLfcMARK2MARK3Rho GTPaseSignalling

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Integrins, such as αvβ3 and α5β1, bind fibronectin (FN) and mediate cellular responses.
  • These integrins influence cell morphology and motility through Rho GTPases.
  • The specific mechanisms linking FN-binding integrins to RhoA activation require further elucidation.

Purpose of the Study:

  • To investigate the role of fibronectin (FN)-binding integrins, specifically αvβ3 and α5β1, in controlling RhoA signaling.
  • To identify the downstream effectors and molecular mechanisms involved in integrin-mediated RhoA activation.
  • To determine the integrin-specific regulation of cellular responses like stress fiber formation and focal adhesion maturation.

Main Methods:

  • Utilized cell culture models to study integrin signaling pathways.
  • Employed techniques to assess RhoA activation, stress fiber formation, and focal adhesion dynamics.
  • Investigated the interaction of Lfc (GEF-H1) with microtubules and its phosphorylation status.
  • Performed gene silencing experiments to evaluate the necessity of Lfc in FN-αvβ3 signaling.

Main Results:

  • FN-bound αvβ3 integrin, but not α5β1, induced Lfc dissociation from microtubules (MTs), activating RhoA.
  • Lfc depletion diminished RhoA activity, stress fiber formation, and focal adhesion (FA) size, identifying Lfc as a key downstream mediator.
  • A kinase cascade involving MARK2 and MARK3 phosphorylated Lfc, with site S151 being critical for Lfc localization and activity.
  • These findings highlight an integrin-specific orchestration of Lfc and RhoA activation in FN-adherent cells.

Conclusions:

  • FN-bound αvβ3 integrin specifically activates RhoA signaling through the dissociation and activation of the RhoA GEF Lfc from microtubules.
  • Lfc is a crucial downstream effector of FN-αvβ3 signaling, regulating RhoA activity, stress fiber assembly, and focal adhesion maturation.
  • The MARK2/MARK3-mediated phosphorylation of Lfc, particularly at S151, is a key regulatory step in this integrin-specific pathway.