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Related Concept Videos

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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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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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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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
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Cell migration, the process by which cells move from one location to another, is essential for the proper development and viability of organisms throughout their life. When cells are not able to migrate properly to their ordained locations, various disorders may occur. For example, disruption in cell migration causes chronic inflammatory diseases such as arthritis.
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Related Experiment Video

Updated: Sep 29, 2025

Imaging CD4 T Cell Interstitial Migration in the Inflamed Dermis
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The Collagen Receptor Discoidin Domain Receptor 1b Enhances Integrin β1-Mediated Cell Migration by Interacting With

Corina M Borza1, Gema Bolas1, Xiuqi Zhang1

  • 1Department of Medicine, Division of Nephrology, Vanderbilt University, Nashville, TN, United States.

Frontiers in Cell and Developmental Biology
|March 21, 2022
PubMed
Summary

Discoidin domain receptor 1 isoform b (DDR1b) enhances cell migration and lung colonization more than DDR1a. DDR1b interacts with talin and BCR, boosting Rac1 activation for improved integrin-mediated cell movement.

Keywords:
Rac1extracellular matrixintegrinsmigrationreceptor activationreceptor tyrosine kinase

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Integrins and discoidin domain receptors (DDRs) mediate cell adhesion and migration on collagen.
  • The specific roles of DDR1 isoforms in cell migration, particularly in relation to integrins, remain unclear.
  • DDR1 has multiple isoforms, with DDR1a and DDR1b being the most common.

Purpose of the Study:

  • To investigate the differential roles of DDR1a and DDR1b isoforms in regulating cell migration on collagen.
  • To elucidate the molecular mechanisms by which DDR1 isoforms influence cell migration and integrin signaling.
  • To identify key proteins involved in the interplay between DDR1 and integrin-mediated cell migration.

Main Methods:

  • Comparison of migration and lung colonization of cells expressing DDR1a versus DDR1b.
  • Biochemical assays using purified recombinant DDR1 cytoplasmic tail proteins to assess talin binding affinity.
  • Immunofluorescence microscopy to visualize colocalization of DDR1 isoforms with talin and integrin β1 at focal adhesions.
  • Analysis of Rac1 activation and interaction with Breakpoint cluster region protein (BCR).

Main Results:

  • DDR1b-expressing cells exhibited significantly enhanced migration on collagen I and DDR-selective substrates compared to DDR1a-expressing cells.
  • DDR1b-expressing cells demonstrated increased lung colonization in vivo.
  • DDR1b directly binds talin with higher affinity than DDR1a, and DDR1b colocalizes with talin and integrin β1 at focal adhesions.
  • DDR1b promotes cell migration by enhancing Rac1 activation through interaction with BCR, reducing its GTPase-activating protein activity.

Conclusions:

  • DDR1b is a key driver of cell migration, surpassing DDR1a in promoting cell movement and metastasis.
  • Talin and BCR are crucial mediators in the functional interplay between DDR1b and integrins, regulating cell migration.
  • Understanding DDR1 isoform-specific functions provides insights into collagen-mediated cell behavior and potential therapeutic targets.