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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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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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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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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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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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Structural aspects of CEACAM1 interactions.

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European Journal of Clinical Investigation
|November 18, 2024
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Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) is a key cell adhesion molecule involved in immune responses and disease. This review details CEACAM1

Keywords:
CEACAM1adhesionhost functionimmune function

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Area of Science:

  • Immunology and Cell Biology
  • Molecular Interactions and Signaling

Background:

  • Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) is a crucial membrane protein with diverse immune and non-immune functions.
  • CEACAM1 acts as both a homophilic and heterophilic ligand, interacting with proteins like CEACAM5, TIM-3, and PD-1.
  • Pathogens exploit CEACAM1 for host invasion and immune evasion, highlighting its clinical relevance in infectious diseases, autoimmunity, and cancer.

Purpose of the Study:

  • To review the structural basis of CEACAM1's homophilic and heterophilic ligand interactions.
  • To discuss the regulation of CEACAM1's monomeric, dimeric, and oligomeric states in cis and trans binding.
  • To explore the downstream signaling consequences and the role of avidity in CEACAM1 activities.

Main Methods:

  • Literature review focusing on structural biology and molecular interactions of CEACAM1.
  • Analysis of CEACAM1's regulatory mechanisms, including cis/trans binding and oligomerization.
  • Exploration of CEACAM1's functional consequences in various biological contexts.

Main Results:

  • Detailed structural insights into CEACAM1's ligand-binding capabilities.
  • Understanding of how CEACAM1's conformational states influence downstream signaling.
  • Identification of avidity as a potential modulator of CEACAM1 function.

Conclusions:

  • CEACAM1's multifaceted interactions and regulatory states are critical for its diverse biological roles.
  • Understanding CEACAM1 structure-function relationships is key to its implications in disease.
  • Further research into CEACAM1 avidity may reveal novel therapeutic strategies.