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Related Experiment Videos

CAM-FGF receptor interactions: a model for axonal growth

P Doherty1, F S Walsh

  • 1Department of Experimental Pathology, UMDS, Guy's Hospital, London, United Kingdom.

Molecular and Cellular Neurosciences
|January 1, 1996
PubMed
Summary

Neural cell adhesion molecules (NCAMs) like N-cadherin and L1 stimulate axonal growth by activating fibroblast growth factor receptors (FGFRs) and a tyrosine kinase-PLCgamma cascade, promoting neurite outgrowth.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Cell adhesion molecules (CAMs) including NCAM, N-cadherin, and L1 are known to stimulate axonal growth.
  • Previous research identified inhibitors of CAM-stimulated neurite outgrowth, implicating a tyrosine kinase-PLCgamma cascade.
  • Integrins were found not to be involved in this specific pathway.

Purpose of the Study:

  • To propose that fibroblast growth factor receptor (FGFR) activation mediates neurite outgrowth stimulated by NCAM, N-cadherin, and L1.
  • To elucidate the downstream signaling events involving PLCgamma, diacylglycerol (DAG), arachidonic acid (AA), and calcium influx.
  • To investigate the potential direct interaction between CAMs and FGFRs based on conserved binding motifs.

Main Methods:

  • Review of existing experimental paradigms and molecular studies on CAMs and neurite outgrowth.

Related Experiment Videos

  • Analysis of signaling pathways, including tyrosine kinase-PLCgamma activation.
  • Examination of evolutionary conservation of binding motifs between CAMs and FGFRs.

    • Main Results:

    • Neurite outgrowth stimulated by NCAM, N-cadherin, and L1 is suggested to be mediated by FGFR activation in neurons.
    • FGFR activation leads to PLCgamma recruitment and activation via SH2 domain interactions.
    • Downstream events include DAG conversion to AA and subsequent calcium influx, crucial for neurite growth.

    Conclusions:

    • The FGFR-PLCgamma cascade is a key pathway for CAM-stimulated neurite outgrowth.
    • Direct interaction between CAMs and FGFRs is proposed, supported by conserved binding motifs.
    • This interaction model provides a basis for predicting other CAMs that may interact with FGFRs.