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Related Experiment Videos

SH2-B and APS are multimeric adapters that augment TrkA signaling.

X Qian1, D D Ginty

  • 1Howard Hughes Medical Institute and the Department of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

Molecular and Cellular Biology
|March 10, 2001
PubMed
Summary

Adapter proteins Src homology 2-B (SH2-B) and APS form multimers that regulate nerve growth factor (NGF) signaling by modulating TrkA receptor activity and neuronal differentiation.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Signaling

Background:

  • Neurotrophins, including nerve growth factor (NGF), are crucial for neuronal development and survival.
  • NGF exerts its effects through Trk receptor tyrosine kinases.
  • Adapter proteins Src homology 2-B (SH2-B) and APS were previously identified as Trk kinase substrates.

Purpose of the Study:

  • To investigate the oligomeric state and functional role of SH2-B and APS in neurotrophin signaling.
  • To determine the specific domains of SH2-B involved in Trk receptor modulation and downstream signaling.
  • To elucidate the mechanism by which SH2-B influences NGF-induced cellular responses.

Main Methods:

  • Cellular assays using PC12 cells.
  • Overexpression of SH2-B and its mutants.

Related Experiment Videos

  • Analysis of TrkA receptor autophosphorylation.
  • Assessment of NGF-mediated morphological differentiation.

    • Main Results:

    • SH2-B and APS exist as stable homopentamers and/or heteropentamers, independent of Trk activation.
    • The N-terminal multimerization domain of SH2-B is essential for its role in NGF signaling.
    • Overexpression of SH2-B enhances the magnitude and duration of TrkA autophosphorylation.
    • The N-terminus of SH2-B is critical for TrkA/SH2-B-mediated PC12 cell differentiation.

    Conclusions:

    • Multimeric adapter proteins SH2-B and APS play a significant role in neurotrophin signaling.
    • These adapters directly modulate Trk receptor autophosphorylation through their N-terminal multimerization domains.
    • SH2-B's multimeric state is key to its function in NGF-induced neuronal survival and differentiation.