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Related Concept Videos

Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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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 Molecules - Types and Functions01:20

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Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
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Adherens Junctions01:24

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Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
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The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
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Related Experiment Video

Updated: Apr 7, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
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CdiA promotes receptor-independent intercellular adhesion.

Zachary C Ruhe1, Loni Townsley2, Adam B Wallace1

  • 1Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA, 93106-9625, USA.

Molecular Microbiology
|July 3, 2015
PubMed
Summary

Contact-dependent growth inhibition (CDI) proteins mediate bacterial competition. CdiA proteins promote bacterial adhesion and auto-aggregation, independent of their toxin activity, enabling cooperative social behaviors.

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Area of Science:

  • Microbiology
  • Bacterial Genetics
  • Cellular Communication

Background:

  • Contact-dependent growth inhibition (CDI) is mediated by CdiB/CdiA proteins, crucial for inter-bacterial competition.
  • CdiA exoproteins deliver toxins to target bacteria, but their role in multicellular behaviors like auto-aggregation and biofilm formation is unclear.

Purpose of the Study:

  • To investigate the role of CdiA-receptor interactions in bacterial biofilm formation and auto-aggregation.
  • To elucidate the mechanisms underlying CdiA-mediated cell-cell adhesion in *Escherichia coli*.

Main Methods:

  • Utilized *Escherichia coli* isolate EC93.
  • Generated and analyzed *cdiA* and *bamA* receptor mutants.
  • Mapped CdiA interaction domains responsible for adhesion.

Main Results:

  • Mutations in *cdiA* and the *bamA* receptor impaired biofilm formation, highlighting CdiA-BamA adhesion.
  • CdiA independently mediated auto-aggregation, suggesting a homotypic CdiA-CdiA interaction.
  • Distinct domains of CdiA mediate BamA-dependent and independent adhesion.

Conclusions:

  • CdiA facilitates bacterial collective behaviors, including adhesion and auto-aggregation, independent of its growth-inhibition function.
  • CdiA-mediated adhesion supports 'greenbeard' discrimination and kin selection, potentially driven by horizontal gene transfer.