Ubiquitination-dependent mechanisms regulate synaptic growth and function

Aaron DiAntonio (), Ali P. Haghighi, Scott L. Portman, Jason D. Lee, Andrew M. Amaranto and Corey S. Goodman
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Aaron DiAntonio: Washington University School of Medicine, 660 S. Euclid, Campus Box 8103
Ali P. Haghighi: University of California, Berkeley, Room 509 Life Sciences Addition
Scott L. Portman: Washington University School of Medicine, 660 S. Euclid, Campus Box 8103
Jason D. Lee: University of California, Berkeley, Room 509 Life Sciences Addition
Andrew M. Amaranto: Washington University School of Medicine, 660 S. Euclid, Campus Box 8103
Corey S. Goodman: University of California, Berkeley, Room 509 Life Sciences Addition

Nature, 2001, vol. 412, issue 6845, 449-452

Abstract: Abstract The covalent attachment of ubiquitin to cellular proteins is a powerful mechanism for controlling protein activity and localization1. Ubiquitination is a reversible modification promoted by ubiquitin ligases and antagonized by deubiquitinating proteases2. Ubiquitin-dependent mechanisms regulate many important processes including cell-cycle progression, apoptosis and transcriptional regulation3. Here we show that ubiquitin-dependent mechanisms regulate synaptic development at the Drosophila neuromuscular junction (NMJ). Neuronal overexpression of the deubiquitinating protease fat facets4 leads to a profound disruption of synaptic growth control; there is a large increase in the number of synaptic boutons, an elaboration of the synaptic branching pattern, and a disruption of synaptic function. Antagonizing the ubiquitination pathway in neurons by expression of the yeast deubiquitinating protease UBP2 (ref. 5) also produces synaptic overgrowth and dysfunction. Genetic interactions between fat facets and highwire6, a negative regulator of synaptic growth that has structural homology to a family of ubiquitin ligases, suggest that synaptic development may be controlled by the balance between positive and negative regulators of ubiquitination.

Date: 2001
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DOI: 10.1038/35086595

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