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The Journal of Neuroscience, June 15, 2001, 21(12):4215-4224

Drosophila - and -Spectrin Mutations Disrupt Presynaptic Neurotransmitter Release

David E. Featherstone¹, Warren S. Davis¹, Ronald R. Dubreuil², and Kendal Broadie¹

¹ Department of Biology, University of Utah, Salt Lake City, Utah 84112-0840, and ² Department of Neurobiology, Pharmacology, and Physiology, University of Chicago, Chicago, Illinois 60637

Spectrins are plasma membrane-associated cytoskeletal proteins implicated in several aspects of synaptic development and function, including presynaptic vesicle tethering and postsynaptic receptor aggregation. To test these hypotheses, we characterized Drosophila mutants lacking either - or -spectrin. The Drosophila genome contains only one -spectrin and one conventional -spectrin gene, making it an ideal system to genetically manipulate spectrin levels and examine the resulting synaptic alterations. Both spectrin proteins are strongly expressed in the Drosophila neuromusculature and highly enriched at the glutamatergic neuromuscular junction. Protein null - and -spectrin mutants are embryonic lethal and display severely disrupted neurotransmission without altered morphological synaptogenesis. Contrary to current models, the absence of spectrins does not alter postsynaptic glutamate receptor field function or the ultrastructural localization of presynaptic vesicles. However, the subcellular localization of numerous synaptic proteins is disrupted, suggesting that the defects in presynaptic neurotransmitter release may be attributable to inappropriate assembly, transport, or localization of proteins required for synaptic function.

Key words: spectrin; Drosophila; synapse; neuromuscular junction; synaptogenesis; cysteine string protein; Discs large; PSD-95; synaptotagmin; synapsin; syntaxin; glutamate receptor

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Copyright © 2001 Society for Neuroscience  0270-6474/01/21124215-10$05.00/0

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