High affinity binding of alpha-latrotoxin to recombinant neurexin I alpha

J Biol Chem. 1995 Oct 13;270(41):23903-5. doi: 10.1074/jbc.270.41.23903.

Abstract

alpha-Latrotoxin is a potent neurotoxin from black widow spider venom that stimulates neurotransmitter release. alpha-Latrotoxin is thought to act by binding to a high affinity receptor on presynaptic nerve terminals. In previous studies, high affinity alpha-latrotoxin binding proteins were isolated and demonstrated to contain neurexin I alpha as a major component. Neurexin I alpha is a cell surface protein that exists in multiple differentially spliced isoforms and belongs to a large family of neuron-specific proteins. Using a series of neurexin I-IgG fusion proteins, we now show that recombinant neurexin I alpha binds alpha-latrotoxin directly with high affinity (Kd approximately 4 nM). Binding of alpha-latrotoxin to recombinant neurexin I alpha is dependent on Ca2+ (EC50 approximately 30 microM). Our data suggest that neurexin I alpha is a Ca(2+)-dependent high affinity receptor for alpha-latrotoxin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing
  • Animals
  • Calcium / pharmacology
  • Cattle
  • Cell Line
  • Chlorocebus aethiops
  • Glycoproteins
  • Humans
  • Immunoglobulin G / biosynthesis
  • Kinetics
  • Nerve Tissue Proteins / biosynthesis
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism*
  • Neuropeptides
  • Neurotoxins / chemistry
  • Neurotoxins / metabolism
  • Protein Binding
  • Rats
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Spider Venoms / chemistry
  • Spider Venoms / metabolism*
  • Transfection

Substances

  • Glycoproteins
  • Immunoglobulin G
  • Nerve Tissue Proteins
  • Neuropeptides
  • Neurotoxins
  • Recombinant Fusion Proteins
  • Recombinant Proteins
  • Spider Venoms
  • neurexophilin
  • alpha-latrotoxin
  • Calcium