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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Structural characterization of the self-association of the death domain of p75(NTR.)

Qianhui Qu1, Jun Chen, Yizhi Wang

  • 1National Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.

Plos One
|March 9, 2013
PubMed

Insights

The neurotrophin receptor p75(NTR) forms novel dimers, revealing insights into its signaling mechanisms. These findings suggest that receptor oligomerization on the cell surface regulates p75(NTR) activity.

Area of Science:

  • Molecular biology
  • Cell signaling
  • Structural biology

Background:

  • The neurotrophin receptor p75(NTR) plays a crucial role in neuronal development and survival.
  • Its intracellular death domain mediates diverse signaling pathways, but its activation mechanism is poorly understood.

Purpose of the Study:

  • To elucidate the structural basis of p75(NTR) death domain activation.
  • To investigate the oligomeric states of p75(NTR) on the cell surface.

Main Methods:

  • X-ray crystallography to determine the structures of the p75(NTR) death domain.
  • Cell surface analysis to study full-length p75(NTR) dimers.

Main Results:

  • Two novel dimer structures of the p75(NTR) death domain were identified: a non-covalent asymmetric dimer and a disulfide-linked symmetric dimer.
  • Both disulfide-linked and non-covalent dimers of full-length p75(NTR) were observed on the cell surface.
  • These oligomeric states differ from those seen in other death domain proteins.

Conclusions:

  • The p75(NTR) death domain can adopt unique dimeric configurations.
  • Multiple p75(NTR) oligomeric states coexist on the cell surface.
  • Neurotrophins or other factors may modulate p75(NTR) signaling by shifting the equilibrium between these oligomeric states.

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