Ubiquitin-Konjugat Bildung und Interaktion mit dem Proteasom (Ubiquitin Conjugate Formation and Proteasome Targeting)

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Selective protein degradation by the ubiquitin/proteasome pathway involves the ubiquitin-conjugation system for substrate recognition and the proteasome for degradation. Recently, we have identified a novel ubiquitination factor, C4 (UFD2), that mediates multiubiquitination in cooperation with E1, E2 and E3 enzymes. E4 interacts with the putative chaperone CDC48, which together with its binding partner UNI2 is required for UFD (ubiquitin fusion) degradation. The central objective of our proposed research is to define the functions of these factors and to establish the sequence of events which lead from the ubiquitination of a substrate to its degradation by the proteasome.