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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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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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Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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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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c-Met and Other Cell Surface Molecules: Interaction, Activation and Functional Consequences.

Giuditta Viticchiè1, Patricia A J Muller2

  • 1MRC (Medical Research Council) Toxicology Unit, Lancaster Road, Leicester LE1 9HN, UK. gv34@le.ac.uk.

Biomedicines
|May 25, 2017
PubMed
Summary

The c-Met receptor (HGF receptor) is crucial for development and cancer. This review details its interactions and crosstalk, clarifying its complex roles in cell signaling, localization, and degradation.

Keywords:
HGF receptorRTKc-Metcrosstalkrecycling

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Area of Science:

  • Cell Biology
  • Molecular Oncology
  • Signal Transduction

Background:

  • The c-Met receptor tyrosine kinase (also known as HGF receptor) is vital in embryonic development, tissue repair, and cancer metastasis.
  • Its precise biological functions and activation mechanisms remain incompletely understood.
  • Aberrant c-Met signaling drives cancer invasion and metastasis through complex kinase cascades.

Purpose of the Study:

  • To review the interactions and crosstalk of the c-Met receptor with various partner molecules.
  • To elucidate the functional consequences of these interactions on c-Met activation, signaling, and intracellular trafficking.
  • To provide a comprehensive overview of c-Met's multifaceted roles in normal physiology and disease.

Main Methods:

  • Literature review of studies on c-Met receptor interactions.
  • Analysis of molecular mechanisms underlying c-Met activation and signaling crosstalk.
  • Examination of c-Met's role in cellular processes like motility, proliferation, and degradation.

Main Results:

  • c-Met interacts with structurally homologous molecules (e.g., plexins) and other receptor tyrosine kinases (e.g., EGFR).
  • These interactions modulate c-Met activation, downstream signaling, intracellular localization, recycling, and degradation.
  • c-Met's crosstalk influences diverse cellular functions, including development, tissue repair, and cancer progression.

Conclusions:

  • Understanding c-Met interactions is key to deciphering its complex biological roles.
  • Modulation of c-Met crosstalk offers potential therapeutic strategies for cancers driven by aberrant signaling.
  • Further research into c-Met's regulatory networks is essential for advancing cancer treatment and regenerative medicine.