Synaptic protein UNC-13 interacts with an F-box protein that may target it for degradation by proteasomes.

  • Cristina Polinsky Department of Biology, Ursinus College, Collegeville, PA, USA.;
  • Chanelle Houston
  • Jaynine Vado
  • Azizahmed Shaikh
  • Rebecca E Kohn

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.
Published
2006-02-23
Section
Articles