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© The Rockefeller University Press, 0021-9525/1998//499 $5.00
The Journal of Cell Biology, Volume 142, Number 2, , 1998 499-509

Articles

Bassoon, a Novel Zinc-finger CAG/Glutamine-repeat Protein Selectively Localized at the Active Zone of Presynaptic Nerve Terminals



Susannetom Dieck*, Lydia Sanmartí-Vila*, Kristina Langnaese*, Karin Richter*, Stefan Kindler{ddagger}, Antje Soyke§, Heike Wex*, Karl-Heinz Smalla*,||, Udo Kämpf*, Jürgen-Theodor Fränzer*, Markus Stumm§, Craig C. Garner, and Eckart D. Gundelfinger*

* Leibniz Institute for Neurobiology, D-39118 Magdeburg, Germany; {ddagger} 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

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.

Key Words: trinucleotide repeats • mouse bassoon gene • presynaptic terminals • rat brain • synapses

Abbreviations used in this paper: aa, amino acid; LIM, lin-11/ISL-1/mec-3-like; MAGUK, membrane-associated guanylate kinase homologue; PSD, postsynaptic density.

S. tom Dieck, L. Sanmartí-Vila, and K. Langnaese contributed equally to this work. The present address of Heike Wex is Department of Human Genetics, Mount Sinai School of Medicine, New York, NY 10029-6514.

Address all correspondence to Eckart D. Gundelfinger, Leibniz Institute for Neurobiology, Postfach 1860, D-39008 Magdeburg, Germany. Tel.: +49-391-6263-228; Fax: +49-391-6263-229; E-mail: gundelfinger{at}ifn-magdeburg.de

2. It should be noted that Bassoon is a presynaptic protein that is highly enriched in the so-called PSD protein fraction. It has been shown previously that presynaptic proteins do occur in this fraction (Langnaese et al., 1996). Another well-documented example of this kind is the presynaptic cytomatrix component Piccolo (Cases-Langhoff et al., 1996). In a recent publication Ziff (1997) provides electron microscopic evidence for the appearence of presynaptic dense projections in the PSD preparation. This indicates that, though the PSD fraction indeed contains primarily postsynaptic proteins (Kennedy, 1997), the name of the fraction may be misleading. Therefore, we refer to this fraction as synaptic junctional protein preparation.


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