Proteolysis of important regulatory proteins by the ubiquitin-proteosome pa
thway is a key aspect of cellular regulation in eukaryotes. Genetic studies
in Arabidopsis indicate that response to auxin depends on the function of
proteins in this pathway. The auxin transport inhibitor resistant 1 (TIR1)
protein is part of a ubiquitin-protein-ligase complex (E3), known as SKP1 C
DC53 F-box(TIR1) (SCFTIR1), that possibly directs ubiquitin-modification of
protein regulators of the auxin response. In yeast, a similar E3 complex,
SCFCDC4, is regulated by conjugation of the ubiquitin-related protein Rub1
to the Cdc53 protein. In Arabidopsis, the AUXIN-RESISTANT1 (AXR1) gene enco
des a subunit of the RUB1-activating enzyme, the first enzyme in the RUB-co
njugation pathway. Loss of AXR1 results in loss of auxin response. These re
sults suggest a model in which RUB1 modification regulates the activity of
SCFTIR1, thereby directing the degradation of the repressors of the auxin r
esponse.