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Volume 16, Number 14,
Issue of July 15, 1996
pp. 4360-4369
Copyright ©1996 Society for Neuroscience
Structure and Evolution of Neurexophilin
Received Feb. 22, 1996; revised April 19, 1996; accepted April 24, 1996.
Alexander G. Petrenko1, 2,
Beate Ullrich1,
Markus Missler1,
Valery Krasnoperov2,
Thomas W. Rosahl1, and
Thomas C. Südhof1
1 Howard Hughes Medical Institute and Department of
Molecular Genetics, The University of Texas Southwestern Medical
School, Dallas, Texas 75235, and 2 Department of
Environmental Medicine, New York University Medical Center, New York,
New York 10016
Using affinity chromatography on immobilized  -latrotoxin, we
have purified a novel 29 kDa protein, neurexophilin, in a complex with
neurexin I. Cloning revealed that rat and bovine neurexophilins are
composed of N-terminal signal peptides, nonconserved N-terminal domains
(20% identity over 80 residues), and highly homologous C-terminal
sequences (85% identity over 169 residues). Analysis of genomic clones
from mice identified two distinct neurexophilin genes, one of which is
more homologous to rat neurexophilin and the other to bovine
neurexophilin. The first neurexophilin gene is expressed abundantly in
adult rat and mouse brain, whereas no mRNA corresponding to the second
gene was detected in rodents despite its abundant expression in bovine
brain, suggesting that rodents and cattle primarily express distinct
neurexophilin genes. RNA blots and in situ hybridizations
revealed that neurexophilin is expressed in adult rat brain at high
levels only in a scattered subpopulation of neurons that probably
represent inhibitory interneurons; by contrast, neurexins are expressed
in all neurons. Neurexophilin contains a signal sequence and is
N-glycosylated at multiple sites, suggesting that it is secreted and
binds to the extracellular domain of neurexin I. This hypothesis was
confirmed by binding recombinant neurexophilin to the extracellular
domains of neurexin I. Together our data suggest that neurexophilin
constitutes a secreted glycoprotein that is synthesized in a subclass
of neurons and may be a ligand for neurexins.
Key words:
neurexins;
-latrotoxin;
synapse;
gene duplication;
neuron-specific receptor;
inhibitory interneurons
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