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[ShcD interacts with TrkC through its PTB and SH2 domains]

Yuan-gang You1, Wei-qi Li, Bin Yin

  • 1National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Beijing 100005, China.

Zhongguo Yi Xue Ke Xue Yuan Xue Bao. Acta Academiae Medicinae Sinicae
|January 19, 2010
PubMed
Abstract

Insights

Shc (Src homology 2 domain-containing) protein D binds to TrkC receptor tyrosine kinase in a manner dependent on TrkC kinase activity. This interaction is mediated by ShcD

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Signaling

Context:

  • Neurotrophin signaling pathways are crucial for neuronal development and function.
  • TrkC receptor tyrosine kinase plays a vital role in the TrkB-Akt signaling cascade.
  • Understanding the molecular interactions governing TrkC signaling is essential for deciphering downstream effects.

Purpose:

  • To investigate the interaction between ShcD and TrkC.
  • To elucidate the molecular mechanisms underlying TrkC downstream signal transduction.
  • To identify the specific domains of ShcD involved in binding to TrkC.

Summary:

  • ShcD interacts with TrkC, but not with a kinase-dead mutant, indicating kinase activity dependence.
  • Both the PTB and SH2 domains of ShcD are involved in binding to TrkC.
  • The PTB domain of ShcD specifically binds to the NPQY motif on TrkC.
  • ShcD and TrkC colocalize in the cytoplasm and plasma membrane of transfected cells.

Impact:

  • Establishes a direct interaction between ShcD and TrkC.
  • Reveals that ShcD binds TrkC in a kinase-activity-dependent manner.
  • Identifies the PTB and SH2 domains of ShcD as key mediators of this interaction.
  • Provides insights into the molecular basis of TrkC signal transduction.

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