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J. Cell Biol.,
Volume 142, Number 2, July 27, 1998 499-509
* Leibniz Institute for Neurobiology, D-39118 Magdeburg, Germany; The molecular architecture of the cytomatrix
of presynaptic nerve terminals is poorly understood.
Here we show that Bassoon, a novel protein of
>400,000 Mr, is a new component of the presynaptic cytoskeleton. The murine bassoon gene maps to chromosome 9F. A comparison with the corresponding rat
cDNA identified 10 exons within its protein-coding region. The Bassoon protein is predicted to contain two
double-zinc fingers, several coiled-coil domains, and a
stretch of polyglutamines (24 and 11 residues in rat and mouse, respectively). In some human proteins, e.g.,
Huntingtin, abnormal amplification of such poly-glutamine regions causes late-onset neurodegeneration.
Bassoon is highly enriched in synaptic protein preparations. In cultured hippocampal neurons, Bassoon colocalizes with the synaptic vesicle protein synaptophysin
and Piccolo, a presynaptic cytomatrix component. At
the ultrastructural level, Bassoon is detected in axon
terminals of hippocampal neurons where it is highly
concentrated in the vicinity of the active zone. Immunogold labeling of synaptosomes revealed that Bassoon
is associated with material interspersed between clear
synaptic vesicles, and biochemical studies suggest a
tight association with cytoskeletal structures. These
data indicate that Bassoon is a strong candidate to be
involved in cytomatrix organization at the site of neurotransmitter release.
Institute for Cellular Biochemistry and Clinical
Neurobiology, University of Hamburg, D-20246 Hamburg, Germany; § Institute for Human Genetics, Medical Faculty, Otto von
Guericke University, D-39120 Magdeburg, Germany; Institute for Pharmacology and Toxicology, Medical Faculty, Otto von
Guericke University, D-39120 Magdeburg, Germany; and ¶ Department of Neurobiology, University of Alabama at Birmingham,
South Birmingham, Alabama 35213-0021
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