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Published Online July 12, 2007
Science DOI: 10.1126/science.1145727

Reports

Submitted on May 29, 2007
Accepted on June 22, 2007

Spatial Regulation of an E3 Ubiquitin Ligase Directs Selective Synapse Elimination

Mei Ding 1, Dan Chao 2, George Wang 1, Kang Shen 2*

1 Department of Biological Sciences
2 Department of Biological Sciences; Neuroscience Program, Stanford University, Stanford, CA 94305, USA.

* To whom correspondence should be addressed.
Kang Shen , E-mail: kangshen{at}stanford.edu

Stereotyped synaptic connectivity can arise both by precise recognition between appropriate partners during synaptogenesis and by selective synapse elimination. The molecular mechanisms that underlie selective synapse removal are largely unknown. Here we report that stereotyped developmental elimination of synapses in the Caenorhabditis elegans hermaphrodite-specific motor neuron (HSNL) was mediated by an SCF complex (E3 ubiquitin ligase) composed of SKR-1 and the F-box protein SEL-10. SYG-1, a synaptic adhesion molecule, bound to SKR-1 and inhibited assembly of the SCF complex, thereby protecting nearby synapses. Thus, subcellular regulation of ubiquitin-mediated protein degradation contributes to precise synaptic connectivity through selective synapse elimination.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)