Published online 22 February 2005. doi:10.1083/jcb.200408157
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 5, 825-836
Molecular dissection of the photoreceptor ribbon synapse
:
physical interaction of Bassoon and RIBEYE is essential for the assembly of the ribbon complex
Susanne tom Dieck1,2,
Wilko D. Altrock2,
Michael M. Kessels2,
Britta Qualmann2,
Hanna Regus1,
Dana Brauner1,
Anna Fejtová2,
Oliver Bracko2,
Eckart D. Gundelfinger2, and
Johann H. Brandstätter1,3
1 Department of Neuroanatomy, Max Planck Institute for Brain Research, D-60528 Frankfurt/Main, Germany
2 Leibniz Institute for Neurobiology, D-39118 Magdeburg, Germany
3 Institute for Zoology, University of Erlangen-Nuernberg, D-91058 Erlangen, Germany
Correspondence to Johann H. Brandstätter: brandstaett{at}mpih-frankfurt.mpg.de
The ribbon complex of retinal photoreceptor synapses represents a specialization of the cytomatrix at the active zone (CAZ) present at conventional synapses. In mice deficient for the CAZ protein Bassoon, ribbons are not anchored to the presynaptic membrane but float freely in the cytoplasm. Exploiting this phenotype, we dissected the molecular structure of the photoreceptor ribbon complex. Identifiable CAZ proteins segregate into two compartments at the ribbon: a ribbon-associated compartment including Piccolo, RIBEYE, CtBP1/BARS, RIM1, and the motor protein KIF3A, and an active zone compartment including RIM2, Munc13-1, a Ca2+ channel
1 subunit, and ERC2/CAST1. A direct interaction between the ribbon-specific protein RIBEYE and Bassoon seems to link the two compartments and is responsible for the physical integrity of the photoreceptor ribbon complex. Finally, we found the RIBEYE homologue CtBP1 at ribbon and conventional synapses, suggesting a novel role for the CtBP/BARS family in the molecular assembly and function of central nervous system synapses.
S. tom Dieck and W.D. Altrock contributed equally to this paper.
Abbreviation used in this paper: CAZ, cytomatrix at the active zone.

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