Functional analysis of SCF ubiquitin ligase complexes

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Ubiquitin-mediated degradation of proteins by the 26S proteasome plays an important role in signaling cascades of many cellular processes in all eukaryotes regulation transcription, DNA replication, cell cycle, differentiation and responses to various exogenous stimuli. The specificity of the ubiquitylation is mediated by different classes of ubiquitin ligases. SCF complexes (for Skp1/Cullin/F-box protein) form one of the most important classes of ubiquitin ligases in eukaryotes, whereby the F-box proteins mediate the specific recognition of target proteins. Because about 2.5 % of all identified Arabidopsis genes encode for putative components of SCF complexes, this class of ubiquitin ligases probably plays an outstanding role in regulating specific protein degradation in higher plants. In the proposed research projects, we want to analyze the function, composition and targets of SCF complexes which carry a member of a certain subfamily of F-box proteins. These F-box proteins show homology to EID1, an important component of phytochrome A-dependent light signaling that was identified from our group. Furthermore, we want to elucidate the specificity of the interaction between the highly variable F-box domains and the components of the core complexes.