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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Structural Basis of p75 Transmembrane Domain Dimerization.

Kirill D Nadezhdin1, Irmina García-Carpio2, Sergey A Goncharuk1

  • 1From the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow 117997, Russian Federation and.

The Journal of Biological Chemistry
|April 9, 2016
PubMed
Summary
This summary is machine-generated.

The p75 neurotrophin receptor

Keywords:
dimerizationneurotrophinnuclear magnetic resonance (NMR)p75 neurotrophin receptortransmembrane domainγ-secretase

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Area of Science:

  • Neuroscience
  • Structural Biology
  • Molecular Biology

Background:

  • Single-span transmembrane receptor activation relies on dimerization.
  • The p75 neurotrophin receptor (p75NTR) is crucial in the nervous system, but its activation mechanism is not fully understood.
  • The transmembrane domain of p75NTR stabilizes receptor dimers via a disulfide bond, which is vital for nerve growth factor (NGF) signaling.

Purpose of the Study:

  • To elucidate the structural basis of p75NTR transmembrane domain dimerization.
  • To investigate the role of Cys(257) and the AXXXG motif in p75NTR structure and function.
  • To understand the mechanism of p75NTR activation in NGF signaling.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to determine the 3D structures of p75-TM-WT and p75-TM-C257A dimers.
  • Reconstitution of receptor dimers in lipid micelles.
  • Biochemical assays and cross-linking experiments.

Main Results:

  • p75-TM-WT forms spontaneous disulfide-linked dimers, with Cys(257) at the dimer interface.
  • Under reducing conditions, p75-TM-WT exists in a monomer-dimer equilibrium.
  • p75-TM-C257A forms dimers via the AXXXG motif, which is not at the dimer interface in p75-TM-WT.
  • The AXXXG motif is involved in regulated intramembrane proteolysis by the γ-secretase complex, not homodimerization.

Conclusions:

  • Cys(257) is key to stabilizing the p75NTR transmembrane dimer in a conformation necessary for NGF signaling.
  • The AXXXG motif's role in proteolysis, rather than dimerization, offers new insights into p75NTR regulation.
  • Structural data reveals the functional significance of specific residues in transmembrane receptor activation.