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The Journal of Neuroscience, November 1, 1999, 19(21):9374-9384

Targeted Expression of Truncated Glued Disrupts Giant Fiber Synapse Formation in Drosophila

Marcus J. Allen¹, Xiaoliang Shan¹, Phyllis Caruccio¹, Stephan J. Froggett¹, Kevin G. Moffat², and R. K. Murphey¹

¹ Department of Biology, Morrill Science Center, University of Massachusetts, Amherst, Massachusetts 01003, and ² Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom

Glued¹ (Gl¹) mutants produce a truncated protein that acts as a poison subunit and disables the cytoplasmic retrograde motor dynein. Heterozygous mutants have axonal defects in the adult eye and the nervous system. Here we show that selective expression of the poison subunit in neurons of the giant fiber (GF) system disrupts synaptogenesis between the GF and one of its targets, the tergotrochanteral motorneuron (TTMn). Growth and pathfinding by the GF axon and the TTMn dendrite are normal, but the terminal of the GF axon fails to develop normally and becomes swollen with large vesicles. This is a presynaptic defect because expression of truncated Glued restricted to the GF results in the same defect. When tested electrophysiologically, the flies with abnormal axons show a weakened or absent GF-TTMn connection. In Glued¹ heterozygotes, GF-TTMn synapse formation appears morphologically normal, but adult flies show abnormal responses to repetitive stimuli. This physiological effect is also observed when tetanus toxin is expressed in the GFs. Because the GF-TTMn is thought to be a mixed electrochemical synapse, the results show that Glued has a role in assembling both the chemical and electrical components. We speculate that disrupting transport of a retrograde signal disrupts synapse formation and maturation.

Key words: retrograde motors; transport; p150^GLUED; giant fibers; UAS-GAL4; dynein-dynactin

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Copyright © 1999 Society for Neuroscience  0270-6474/99/19219374-11$05.00/0

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