Work

High Affinity Binding of α-Latrotoxin to Recombinant Neurexin Iα

Year: 1995

Type: article

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.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.270.41.23903

Authors: Bazbek A. Davletov, Valery Krasnoperov, Yutaka Hata, Alexander G. Petrenko, Thomas C. Südhof

Institutions: Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, NYU Langone Health, New York University

Language: English

Topic: Venomous Animal Envenomation and Studies

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430