Published 23 May 2005. doi:10.1083/jcb.200502115
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 4, 669-680
Structurally and functionally unique complexins at retinal ribbon synapses
Kerstin Reim1,
Heike Wegmeyer1,
Johann Helmut Brandstätter2,7,
Mingshan Xue3,4,
Christian Rosenmund3,4,
Thomas Dresbach5,
Kay Hofmann6, and
Nils Brose1
1 Department of Molecular Neurobiology, Max-Planck-Institute for Experimental Medicine, D-37075 Göttingen, Germany
2 Department of Neuroanatomy, Max-Planck-Institute for Brain Research, D-60528 Frankfurt/Main, Germany
3 Department of Neuroscience, Houston, TX 77030
4 Department of Molecular and Human Genetics Baylor College of Medicine, Houston, TX 77030
5 Institute for Anatomy and Cell Biology, Ruprecht-Karls-University Heidelberg, D-69120 Heidelberg, Germany
6 Bioinformatics Group, MEMOREC Biotech GmbH, D-50829 Köln, Germany
7 Institute for Zoology, University of Erlangen-Nürnberg, D-91058 Erlangen, Germany
Correspondence to Nils Brose: brose{at}em.mpg.de
Ribbon synapses in retinal sensory neurons maintain large pools of readily releasable synaptic vesicles. This allows them to release several hundreds of vesicles per second at every presynaptic release site. The molecular components that cause this high transmitter release efficiency of ribbon synapses are unknown. In the present study, we identified and characterized two novel vertebrate complexins (CPXs), CPXs III and IV, that are the only CPX isoforms present in retinal ribbon synapses. CPXs III and IV are COOH-terminally farnesylated, and, like CPXs I and II, bind to SNAP receptor complexes. CPXs III and IV can functionally replace CPXs I and II, and their COOH-terminal farnesylation regulates their synaptic targeting and modulatory function in transmitter release. The novel CPXs III and IV may contribute to the unique release efficacy of retinal sensory neurons.
K. Reim, H. Wegmeyer, J.H. Brandstätter, and M. Xue contributed equally to this work.
Abbreviations used in this paper: CPX, complexin; DIV, d in vitro; DKO, double KO; GCL, ganglion cell layer; INL, inner nuclear layer; IPL, inner plexiform layer; KO, knockout; OPL, outer plexiform layer; PNA, peanut agglutinin; RRP, readily releasable vesicle pool; SNAP-25, synaptosomal-associated protein of 25 kD; wt, wild-type.

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