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MBC in Press, published online ahead of print January 4, 2006
Mol. Biol. Cell 10.1091/mbc.E05-08-0794

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Submitted on August 24, 2005
Revised on December 5, 2005
Accepted on December 27, 2005

KEL-8 Is a Substrate Receptor for CUL3-dependent Ubiquitin Ligase That Regulates Synaptic Glutamate Receptor Turnover

Henry Schaefer and Christopher Rongo

The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854

Monitoring Editor: Ben Margolis

The regulated localization of AMPA-type glutamate receptors (AMPARs) to synapses is an important component of synaptic signaling and plasticity. Regulated ubiquitination and endocytosis determine the synaptic levels of AMPARs, but it is unclear which factors conduct these processes. To identify genes that regulate AMPAR synaptic abundance, we screened for mutants that accumulate high synaptic levels of the AMPAR subunit GLR-1 in C. elegans. GLR-1 is localized to postsynaptic clusters, and mutants for the BTB-Kelch protein KEL-8 have increased GLR-1 levels at clusters, whereas the levels and localization of other synaptic proteins appear normal. KEL-8 is a neuronal protein, and is localized to sites adjacent to GLR-1 postsynaptic clusters along the ventral cord neurites. KEL-8 is required for the ubiquitin-mediated turnover of GLR-1 subunits, and kel-8 mutants show an increased frequency of spontaneous reversals in locomotion, suggesting increased levels of GLR-1 are present at synapses. KEL-8 binds to CUL-3, a Cullin 3 ubiquitin ligase subunit that we also find mediates GLR-1 turnover. Our findings indicate that KEL-8 is a substrate receptor for Cullin 3 ubiquitin ligases that is required for the proteolysis of GLR-1 receptors, and suggest a novel postmitotic role in neurons for Kelch/CUL3 ubiquitin ligases.

Address correspondence to: Christopher Rongo (rongo{at}waksman.rutgers.edu)




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