Synaptic protein UNC-13 interacts with an F-box protein that may target it for degradation by proteasomes
Polinsky, C.; Houston, C.; Vado, J.; Shaikh, A.; Kohn, R.E.
Acta Biochimica Polonica 53(1): 145-148
2006
ISSN/ISBN: 0001-527X PMID: 16496042 Document Number: 595501
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.