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Updated: Aug 11, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
Published on: March 26, 2014
Synaptic protein UNC-13 interacts with an F-box protein that may target it for degradation by proteasomes
Cristina Polinsky1, Chanelle Houston, Jaynine Vado
1Department of Biology, Ursinus College, Collegeville, PA, USA.
Abstract:
UNC-13 protein participates in regulating neurotransmitter release. In Drosophila melanogaster, proteasomal degradation controls UNC-13 levels at synapses. Function of the amino-terminal region of a 207 kDa form of Caenorhabditis elegans UNC-13 is unknown. Yeast two-hybrid and secondary yeast assays identified an F-box protein that interacts with this amino-terminal region. As F-box proteins bind proteins targeted for proteasomal degradation, this protein may participate in degrading a subset of UNC-13 proteins, suggesting that different forms of UNC-13 are regulated differently. Yeast assays also identified an exonuclease, a predicted splicing factor, and a protein with coiled-coil domains, indicating that UNC-13 may affect RNA function.
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