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Ubiquitination is a posttranslational modification that the substrate proteins are covalently conjugated with an ubiquitin or a polyubiquitin chain. Ubiquitination regulates a wide range of cellular progresses including cell cycle progression, transcription and antigen processing in both proteasome dependent and independent manner. Recent findings also substantiate many essential roles of ubiquitination in the regulation of apoptosis. In this thesis, I report my studies on how ubiquitination controls the stability and functions of proteins involved in apoptosis. Livin is a member of the IAP (Inhibitor of apoptosis protein) family. It has been reported that Livin inhibits caspase-3 and -7 in vitro and caspase-9 in vivo and is negatively regulated by Smac/DIABLO (Second mitochondria derived activator of caspases/Direct IAP binding protein with low PI). However the detailed mechanism underlying its anti-apoptotic function has not yet been fully characterized. In the first part of my thesis, the anti-apoptotic function of Livin through its ability to ubiquitinate and degrade death inducer Smac is presented. In summary, it was found that Livin can act as an E3 ubiquitin ligase to target Smac or itself for degradation by the proteasome. RING domain mediated E3 ligase activity is essential for the autoubiquitination and rapid degradation of Livin under normal state. However upon apoptotic stimulation, Livin promotes degradation of its antagonist Smac by accelerating the ubiquitination process.

Regulation of apoptosis by ubiquitination : the functional consequences after Livin associates with SMAC/DIABLO; ARF complexes with COMMD1