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

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Polinsky C., Houston C., Vado J., Shaikh A., Kohn R. E.

Acta Biochimica Polonica

2006

tom 53

nr 1

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.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Houston C.

1 Kohn R. E.

1 Polinsky C.

1 Shaikh A.

1 Vado J.

1 2006

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