TSG101 exhibits multiple functions, including vesicular trafficking, cell growth, differentiation, and transcriptional regulation. However, the cellular signaling that regulates TSG101 functions remains unexplored. Our previous result indicates that TSG101 can be phosphorylated by PKC and GSK3£]. In this thesis, we further investigate the detail phosphorylated amino acid residues by using in vitro kinase assay in conjunction with MALDI-TOF and peptide array analysis. The results indicate that S13, S48, S103 and S367, T383 residues could be phosphorylated by PKC, S182 and S212 by GSK3£].
Coiled-coil domain of TSG101, which contains 2 consensus CK¢º phosphorylation sites,could be phosphorylated by CK¢º. These results indicate the functions of TSG101 might be regulated by these kinases.
Proteasome mediated protein degradation is important to maintain proper cellular functions including cell growth, differentiation and signaling associated with cell cycle control. Impaired function of this system has been implicated in human diseases associated with neurodegeneration and cancer. The inhibitor of proteasome has been successfully used in treatment of these related diseases. In this thesis, we successfully established Ub-X-GFP reporter cell lines, which could be used in the future study on the functional role of TSG101, an E2 variant, in the proteasome mediated degradation pathway. Furthermore, these cell lines will serve a useful cellular platform for screening new proteasome inhibitors.
| Identifer | oai:union.ndltd.org:NSYSU/oai:NSYSU:etd-0913106-174844 |
| Date | 13 September 2006 |
| Creators | Chen, Chao-hui |
| Contributors | Jiin-Tsuey Cheng, Ching-Mei Hsu, none |
| Publisher | NSYSU |
| Source Sets | NSYSU Electronic Thesis and Dissertation Archive |
| Language | Cholon |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0913106-174844 |
| Rights | restricted, Copyright information available at source archive |
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